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Entry: 5EAI
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HEADER    OXIDOREDUCTASE                          16-OCT-15   5EAI              
TITLE     CRYSTAL STRUCTURE OF NAD(P)H DEHYDROGENASE, QUINONE 1 COMPLEXED WITH A
TITLE    2 CHEMOTHERAPEUTIC NAPHTHOQUINONE E6A                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NAD(P)H DEHYDROGENASE [QUINONE] 1;                         
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N;                     
COMPND   4 SYNONYM: AZOREDUCTASE,DT-DIAPHORASE,DTD,MENADIONE REDUCTASE,NAD(P)   
COMPND   5 H:QUINONE OXIDOREDUCTASE 1,PHYLLOQUINONE REDUCTASE,QUINONE REDUCTASE 
COMPND   6 1,QR1;                                                               
COMPND   7 EC: 1.6.5.2;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NQO1, DIA4, NMOR1;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: 19-PPS                                    
KEYWDS    NQO1, TWO-ELECTRON REDUCTION OF QUINONE, NAD(P)H DEHYDROGENASE,       
KEYWDS   2 DIMERIC NAPHTHOQUINONE, OXIDOREDUCTASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.S.PIDUGU,J.E.MBIMBA,M.AHMAD,E.POZHARSKI,E.A.SAUSVILLE,A.EMADI,      
AUTHOR   2 E.A.TOTH                                                             
REVDAT   1   17-FEB-16 5EAI    0                                                
JRNL        AUTH   L.S.PIDUGU,J.C.MBIMBA,M.AHMAD,E.POZHARSKI,E.A.SAUSVILLE,     
JRNL        AUTH 2 A.EMADI,E.A.TOTH                                             
JRNL        TITL   A DIRECT INTERACTION BETWEEN NQO1 AND A CHEMOTHERAPEUTIC     
JRNL        TITL 2 DIMERIC NAPHTHOQUINONE.                                      
JRNL        REF    BMC STRUCT.BIOL.              V.  16     1 2016              
JRNL        REFN                   ESSN 1472-6807                               
JRNL        PMID   26822308                                                     
JRNL        DOI    10.1186/S12900-016-0052-X                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 95.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 102741                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.185                          
REMARK   3   R VALUE            (WORKING SET)  : 0.183                          
REMARK   3   FREE R VALUE                      : 0.220                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.840                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 4972                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.90                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.98                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.94                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 7501                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2540                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 7147                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2517                   
REMARK   3   BIN FREE R VALUE                        : 0.3025                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.72                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 354                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 30099                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 872                                     
REMARK   3   SOLVENT ATOMS            : 50                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 71.98                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 73.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.32110                                             
REMARK   3    B22 (A**2) : 23.99540                                             
REMARK   3    B33 (A**2) : -23.67430                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.422               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.338               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.917                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 31861  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 43245  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 10882  ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 692    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 5076   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 31861  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 4017   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 36113  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.13                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.92                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.65                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|3 - A|272 A|601 - A|601 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -24.2014   17.6576  -17.7094           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1005 T22:   -0.0915                                    
REMARK   3     T33:   -0.2035 T12:   -0.0719                                    
REMARK   3     T13:   -0.0039 T23:   -0.0653                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2454 L22:    3.2934                                    
REMARK   3     L33:    0.9450 L12:   -0.0063                                    
REMARK   3     L13:   -0.1424 L23:   -0.1272                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1313 S12:   -0.1125 S13:    0.0829                     
REMARK   3     S21:    0.2615 S22:   -0.0821 S23:    0.0054                     
REMARK   3     S31:   -0.0716 S32:    0.1029 S33:   -0.0493                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|3 - B|272 B|301 - B|301 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -39.5624   17.5495  -33.4547           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0514 T22:   -0.1889                                    
REMARK   3     T33:   -0.0514 T12:    0.0263                                    
REMARK   3     T13:   -0.1230 T23:   -0.0065                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0500 L22:    3.6145                                    
REMARK   3     L33:    1.3921 L12:    0.5846                                    
REMARK   3     L13:   -0.2838 L23:    0.0155                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0278 S12:    0.0769 S13:    0.2098                     
REMARK   3     S21:   -0.5954 S22:    0.0184 S23:    0.7223                     
REMARK   3     S31:   -0.0151 S32:   -0.0747 S33:   -0.0462                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|1 - C|272 C|601 - C|601 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -62.5463   16.5170  -95.2298           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0695 T22:   -0.0470                                    
REMARK   3     T33:   -0.1951 T12:    0.0039                                    
REMARK   3     T13:   -0.0379 T23:   -0.0087                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9160 L22:    3.9568                                    
REMARK   3     L33:    1.5781 L12:    0.3897                                    
REMARK   3     L13:   -0.3154 L23:    0.1268                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1041 S12:    0.0857 S13:    0.2108                     
REMARK   3     S21:   -0.2257 S22:   -0.1193 S23:    0.1738                     
REMARK   3     S31:    0.1975 S32:   -0.1421 S33:    0.0152                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|3 - D|273 D|301 - D|301 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -46.9971   18.6646  -79.5326           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0438 T22:   -0.0677                                    
REMARK   3     T33:   -0.0874 T12:   -0.0513                                    
REMARK   3     T13:   -0.0869 T23:   -0.0125                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9090 L22:    2.9772                                    
REMARK   3     L33:    1.1533 L12:    0.0633                                    
REMARK   3     L13:   -0.5538 L23:   -0.1639                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1465 S12:   -0.2586 S13:    0.1660                     
REMARK   3     S21:    0.5759 S22:   -0.1825 S23:   -0.5624                     
REMARK   3     S31:    0.0917 S32:    0.2140 S33:    0.0360                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { E|2 - E|272 E|601 - E|601 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -37.1970  -25.7305  -32.0649           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1579 T22:   -0.0941                                    
REMARK   3     T33:   -0.0337 T12:   -0.0481                                    
REMARK   3     T13:   -0.0341 T23:   -0.0107                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.1211 L22:    3.7332                                    
REMARK   3     L33:    1.2369 L12:    0.2997                                    
REMARK   3     L13:    0.2576 L23:   -0.1653                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1899 S12:    0.1845 S13:   -0.0869                     
REMARK   3     S21:   -0.3513 S22:    0.0414 S23:    0.2803                     
REMARK   3     S31:   -0.2112 S32:    0.0940 S33:    0.1485                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { F|2 - F|272 F|301 - F|301 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -38.7900  -28.7434  -10.2233           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0629 T22:   -0.0762                                    
REMARK   3     T33:   -0.0666 T12:   -0.0613                                    
REMARK   3     T13:    0.0642 T23:    0.0627                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.0250 L22:    2.6054                                    
REMARK   3     L33:    1.2456 L12:    0.0588                                    
REMARK   3     L13:    0.1815 L23:   -0.1597                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0234 S12:   -0.4103 S13:   -0.1021                     
REMARK   3     S21:    0.6274 S22:   -0.0999 S23:    0.1474                     
REMARK   3     S31:   -0.0946 S32:   -0.1220 S33:    0.0765                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { G|1 - G|272 G|601 - G|601 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -18.1152  -41.2276  -99.2691           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0046 T22:   -0.0271                                    
REMARK   3     T33:   -0.2484 T12:    0.1278                                    
REMARK   3     T13:    0.0524 T23:    0.0455                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.5157 L22:    2.3750                                    
REMARK   3     L33:    1.5595 L12:   -0.8413                                    
REMARK   3     L13:   -0.0278 L23:   -0.7201                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0958 S12:    0.6459 S13:   -0.1266                     
REMARK   3     S21:   -0.5240 S22:   -0.1818 S23:    0.0739                     
REMARK   3     S31:    0.2854 S32:    0.0793 S33:    0.0860                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { H|2 - H|272 H|301 - H|301 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -16.0091  -38.2563  -77.4003           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0710 T22:   -0.0226                                    
REMARK   3     T33:   -0.2473 T12:    0.0497                                    
REMARK   3     T13:    0.1099 T23:    0.0833                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.5966 L22:    4.1066                                    
REMARK   3     L33:    0.8173 L12:   -1.2765                                    
REMARK   3     L13:    0.1610 L23:   -0.4853                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1259 S12:   -0.4252 S13:    0.1129                     
REMARK   3     S21:    0.1606 S22:    0.1013 S23:    0.1938                     
REMARK   3     S31:   -0.1391 S32:    0.1319 S33:    0.0246                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: { I|1 - I|272 I|601 - I|601 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -64.7774  -27.4821  -77.3152           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0034 T22:   -0.1050                                    
REMARK   3     T33:   -0.1078 T12:   -0.0068                                    
REMARK   3     T13:    0.0005 T23:    0.0497                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7305 L22:    3.1027                                    
REMARK   3     L33:    1.0279 L12:    0.3186                                    
REMARK   3     L13:    0.1106 L23:   -0.1712                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0393 S12:   -0.2191 S13:   -0.1404                     
REMARK   3     S21:    0.2983 S22:   -0.1059 S23:    0.1174                     
REMARK   3     S31:    0.0847 S32:   -0.0787 S33:    0.1452                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: { J|2 - J|272 J|301 - J|301 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -62.8643  -26.7078  -99.4624           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0552 T22:   -0.1361                                    
REMARK   3     T33:   -0.0972 T12:    0.0282                                    
REMARK   3     T13:   -0.0334 T23:    0.0112                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6987 L22:    2.4506                                    
REMARK   3     L33:    1.1647 L12:    0.0748                                    
REMARK   3     L13:    0.0707 L23:   -0.2486                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0723 S12:    0.1624 S13:   -0.0742                     
REMARK   3     S21:   -0.4131 S22:   -0.0507 S23:    0.2425                     
REMARK   3     S31:    0.0603 S32:    0.0795 S33:    0.1230                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: { K|2 - K|272 K|601 - K|601 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -85.8517  -36.3897  -34.2076           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1264 T22:   -0.0019                                    
REMARK   3     T33:   -0.1638 T12:   -0.0506                                    
REMARK   3     T13:    0.1094 T23:   -0.0656                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.1930 L22:    3.2046                                    
REMARK   3     L33:    1.3401 L12:   -0.1867                                    
REMARK   3     L13:    0.0510 L23:    0.2866                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0363 S12:    0.6861 S13:   -0.1789                     
REMARK   3     S21:   -0.5333 S22:   -0.0039 S23:   -0.2236                     
REMARK   3     S31:   -0.0300 S32:   -0.1067 S33:    0.0401                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: { L|1 - L|273 L|301 - L|301 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -84.0691  -42.2403  -12.8779           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2225 T22:   -0.1619                                    
REMARK   3     T33:    0.0535 T12:   -0.0743                                    
REMARK   3     T13:    0.0467 T23:    0.0745                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.4401 L22:    2.4575                                    
REMARK   3     L33:    1.7800 L12:   -0.0622                                    
REMARK   3     L13:   -0.1069 L23:   -0.0233                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1119 S12:   -0.1922 S13:   -0.4731                     
REMARK   3     S21:    0.1532 S22:   -0.0493 S23:   -0.1088                     
REMARK   3     S31:    0.2670 S32:    0.0285 S33:    0.1612                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: { M|1 - M|273 M|601 - M|601 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -96.9524   30.6015  -65.6165           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0349 T22:   -0.1085                                    
REMARK   3     T33:   -0.1206 T12:    0.0249                                    
REMARK   3     T13:    0.0545 T23:   -0.0524                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.8992 L22:    1.2316                                    
REMARK   3     L33:    2.1474 L12:    0.2362                                    
REMARK   3     L13:   -1.0962 L23:    0.2034                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1412 S12:    0.4051 S13:    0.2294                     
REMARK   3     S21:   -0.3992 S22:    0.0078 S23:    0.1954                     
REMARK   3     S31:   -0.1014 S32:   -0.2710 S33:   -0.1489                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: { N|2 - N|272 N|301 - N|301 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -83.8035   28.7339  -47.9494           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0902 T22:   -0.0466                                    
REMARK   3     T33:   -0.1202 T12:   -0.0424                                    
REMARK   3     T13:    0.0570 T23:   -0.1272                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9887 L22:    2.8026                                    
REMARK   3     L33:    2.2406 L12:   -0.4993                                    
REMARK   3     L13:   -0.9093 L23:    1.1908                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0943 S12:   -0.5113 S13:    0.0842                     
REMARK   3     S21:    0.1478 S22:    0.2202 S23:   -0.4572                     
REMARK   3     S31:    0.0994 S32:    0.2375 S33:   -0.3145                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5EAI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214590.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 102839                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 95.670                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, SODIUM POTASSIUM TARTARATE,     
REMARK 280  PH 7.5, VAPOR DIFFUSION, SITTING DROP                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       47.80000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      114.04000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      105.38500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      114.04000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       47.80000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      105.38500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7                                     
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     VAL A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     LYS A   273                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     VAL B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     LYS B   273                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     PRO C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     MET C     0                                                      
REMARK 465     LYS C   273                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     PRO D    -2                                                      
REMARK 465     HIS D    -1                                                      
REMARK 465     MET D     0                                                      
REMARK 465     VAL D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     GLY E    -3                                                      
REMARK 465     PRO E    -2                                                      
REMARK 465     HIS E    -1                                                      
REMARK 465     MET E     0                                                      
REMARK 465     VAL E     1                                                      
REMARK 465     LYS E   273                                                      
REMARK 465     GLY F    -3                                                      
REMARK 465     PRO F    -2                                                      
REMARK 465     HIS F    -1                                                      
REMARK 465     MET F     0                                                      
REMARK 465     VAL F     1                                                      
REMARK 465     LYS F   273                                                      
REMARK 465     GLY G    -3                                                      
REMARK 465     PRO G    -2                                                      
REMARK 465     HIS G    -1                                                      
REMARK 465     MET G     0                                                      
REMARK 465     LYS G   273                                                      
REMARK 465     GLY H    -3                                                      
REMARK 465     PRO H    -2                                                      
REMARK 465     HIS H    -1                                                      
REMARK 465     MET H     0                                                      
REMARK 465     VAL H     1                                                      
REMARK 465     LYS H   273                                                      
REMARK 465     GLY I    -3                                                      
REMARK 465     PRO I    -2                                                      
REMARK 465     HIS I    -1                                                      
REMARK 465     MET I     0                                                      
REMARK 465     LYS I   273                                                      
REMARK 465     GLY J    -3                                                      
REMARK 465     PRO J    -2                                                      
REMARK 465     HIS J    -1                                                      
REMARK 465     MET J     0                                                      
REMARK 465     VAL J     1                                                      
REMARK 465     LYS J   273                                                      
REMARK 465     GLY K    -3                                                      
REMARK 465     PRO K    -2                                                      
REMARK 465     HIS K    -1                                                      
REMARK 465     MET K     0                                                      
REMARK 465     VAL K     1                                                      
REMARK 465     LYS K   273                                                      
REMARK 465     GLY L    -3                                                      
REMARK 465     PRO L    -2                                                      
REMARK 465     HIS L    -1                                                      
REMARK 465     MET L     0                                                      
REMARK 465     GLY M    -3                                                      
REMARK 465     PRO M    -2                                                      
REMARK 465     HIS M    -1                                                      
REMARK 465     MET M     0                                                      
REMARK 465     GLY N    -3                                                      
REMARK 465     PRO N    -2                                                      
REMARK 465     HIS N    -1                                                      
REMARK 465     MET N     0                                                      
REMARK 465     VAL N     1                                                      
REMARK 465     LYS N   273                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A 194    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE A 214    CG1  CG2  CD1                                       
REMARK 470     PHE A 232    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  22    CG   CD   CE   NZ                                   
REMARK 470     LYS B  30    CG   CD   CE   NZ                                   
REMARK 470     LYS B  53    CG   CD   CE   NZ                                   
REMARK 470     ASN B  64    CG   OD1  ND2                                       
REMARK 470     LYS B  76    CG   CD   CE   NZ                                   
REMARK 470     TYR B 128    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS C  53    CG   CD   CE   NZ                                   
REMARK 470     ASN E  64    CG   OD1  ND2                                       
REMARK 470     ARG F   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL G   1    CG1  CG2                                            
REMARK 470     TYR G 128    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU G 185    CG   CD   OE1  OE2                                  
REMARK 470     ASP G 198    CG   OD1  OD2                                       
REMARK 470     PHE G 232    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN G 233    CG   CD   OE1  NE2                                  
REMARK 470     VAL I   1    CG1  CG2                                            
REMARK 470     ASN J  64    CG   OD1  ND2                                       
REMARK 470     TYR J 128    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN K 233    CG   CD   OE1  NE2                                  
REMARK 470     TYR L 128    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN L 233    CG   CD   OE1  NE2                                  
REMARK 470     LYS M  58    CG   CD   CE   NZ                                   
REMARK 470     LYS M  60    CG   CD   CE   NZ                                   
REMARK 470     LYS M 240    CG   CD   CE   NZ                                   
REMARK 470     GLU M 241    CG   CD   OE1  OE2                                  
REMARK 470     GLN M 243    CG   CD   OE1  NE2                                  
REMARK 470     LYS M 247    CG   CD   CE   NZ                                   
REMARK 470     ARG N   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG N  14    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS N  31    CG   CD   CE   NZ                                   
REMARK 470     ASN N 248    CG   OD1  ND2                                       
REMARK 470     ARG N 272    CG   CD   NE   CZ   NH1  NH2                        
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     ARG B   272                                                      
REMARK 475     VAL C     1                                                      
REMARK 475     GLY F     2                                                      
REMARK 475     ARG J   272                                                      
REMARK 475     VAL L     1                                                      
REMARK 475     VAL M     1                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A   14   NE   CZ   NH1  NH2                                  
REMARK 480     LYS A   30   CD   CE   NZ                                        
REMARK 480     LYS A   31   CG   CD   CE   NZ                                   
REMARK 480     LYS A   32   CD   CE   NZ                                        
REMARK 480     LYS A   53   CG   CD   CE   NZ                                   
REMARK 480     LYS A   58   CD   CE   NZ                                        
REMARK 480     LYS A   60   CD   CE   NZ                                        
REMARK 480     LYS A   76   CG   CD   CE   NZ                                   
REMARK 480     LYS A  209   CG   CD   CE   NZ                                   
REMARK 480     GLN A  233   CB   CG   CD   OE1  NE2                             
REMARK 480     LYS A  240   CD   CE   NZ                                        
REMARK 480     LYS A  247   CD   CE   NZ                                        
REMARK 480     ARG A  272   CZ   NH1  NH2                                       
REMARK 480     ARG B    4   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG B   14   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS B   31   CD   CE   NZ                                        
REMARK 480     LYS B   32   CG   CD   CE   NZ                                   
REMARK 480     GLU B   35   CG   CD   OE1  OE2                                  
REMARK 480     LYS B   58   CG   CD   CE   NZ                                   
REMARK 480     LYS B   60   CD   CE   NZ                                        
REMARK 480     LYS B   76   C    O                                              
REMARK 480     LYS B  134   CB   CG   CD   CE   NZ                              
REMARK 480     LYS B  141   CB   CG   CD   CE   NZ                              
REMARK 480     ASP B  198   CB   CG   OD1  OD2                                  
REMARK 480     GLU B  205   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  208   CG   CD   CE   NZ                                   
REMARK 480     LYS B  209   CG   CD   CE   NZ                                   
REMARK 480     LYS B  240   CE   NZ                                             
REMARK 480     LYS B  247   CG   CD   CE   NZ                                   
REMARK 480     ASN B  248   CB   CG   OD1  ND2                                  
REMARK 480     ARG C    3   CG   CD   NE   CZ   NH1                             
REMARK 480     ARG C   14   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS C   31   CE   NZ                                             
REMARK 480     LYS C   58   CG   CD   CE   NZ                                   
REMARK 480     LYS C   60   CE   NZ                                             
REMARK 480     TYR C  128   CD2  CE2  CZ   OH                                   
REMARK 480     GLN C  202   CG   CD   OE1  NE2                                  
REMARK 480     LYS C  209   CG   CD   CE   NZ                                   
REMARK 480     PHE C  232   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     GLN C  233   CB   CG   CD   OE1  NE2                             
REMARK 480     LYS C  240   CD   CE   NZ                                        
REMARK 480     LYS C  247   CG   CD   CE   NZ                                   
REMARK 480     ARG C  272   CD   NE   CZ   NH1  NH2                             
REMARK 480     ARG D    3   CZ   NH1  NH2                                       
REMARK 480     LYS D   30   CG   CD   CE   NZ                                   
REMARK 480     LYS D   31   CE   NZ                                             
REMARK 480     LYS D   32   CG   CD   CE   NZ                                   
REMARK 480     LYS D   53   CD   CE   NZ                                        
REMARK 480     LYS D   58   CD   CE   NZ                                        
REMARK 480     LYS D   60   CE   NZ                                             
REMARK 480     TYR D  128   OH                                                  
REMARK 480     LYS D  134   NZ                                                  
REMARK 480     ILE D  201   CG1  CG2  CD1                                       
REMARK 480     LYS D  208   CG   CD   CE   NZ                                   
REMARK 480     LYS D  209   CG   CD   CE   NZ                                   
REMARK 480     LEU D  211   CD1  CD2                                            
REMARK 480     LYS D  240   NZ                                                  
REMARK 480     LYS D  247   CD   NZ                                             
REMARK 480     LYS D  250   CD   CE   NZ                                        
REMARK 480     ARG D  272   CZ   NH1  NH2                                       
REMARK 480     LYS E   31   CE   NZ                                             
REMARK 480     LYS E   32   CE   NZ                                             
REMARK 480     LYS E   53   CD   CE   NZ                                        
REMARK 480     LYS E   58   CB   CG   CD   CE   NZ                              
REMARK 480     LYS E   60   CE   NZ                                             
REMARK 480     LEU E   73   CG   CD1  CD2                                       
REMARK 480     LYS E   76   CD   CE   NZ                                        
REMARK 480     TYR E  128   CD1  CE1  CZ   OH                                   
REMARK 480     LYS E  134   CD   CE   NZ                                        
REMARK 480     LYS E  209   CG   CD   CE   NZ                                   
REMARK 480     GLN E  233   CG   CD   OE1  NE2                                  
REMARK 480     LYS E  247   CG   CD   CE   NZ                                   
REMARK 480     ASN E  248   CG   OD1  ND2                                       
REMARK 480     LYS E  249   CE   NZ                                             
REMARK 480     LYS E  250   CG   CD   CE   NZ                                   
REMARK 480     ARG E  272   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     ARG F    4   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG F   14   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS F   31   CE   NZ                                             
REMARK 480     LYS F   32   CB   CG   CD   CE   NZ                              
REMARK 480     LYS F   58   CD   CE   NZ                                        
REMARK 480     LYS F   60   CD   CE   NZ                                        
REMARK 480     GLU F   92   CD   OE1  OE2                                       
REMARK 480     TYR F  128   CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 480     LYS F  134   CD   CE   NZ                                        
REMARK 480     GLN F  202   CG   CD   OE1  NE2                                  
REMARK 480     LYS F  209   CG   CD   CE   NZ                                   
REMARK 480     LYS F  240   CG   CD   CE   NZ                                   
REMARK 480     LYS F  247   CD   CE   NZ                                        
REMARK 480     ARG F  272   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     VAL G    1   N    CA   CB                                        
REMARK 480     ARG G    4   CD   NE   CZ   NH1  NH2                             
REMARK 480     ARG G   14   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     LYS G   32   CD   CE   NZ                                        
REMARK 480     LYS G   58   CG   CD   CE   NZ                                   
REMARK 480     LYS G   60   CE   NZ                                             
REMARK 480     LYS G   76   CD   CE   NZ                                        
REMARK 480     HIS G   79   ND1  CD2  CE1  NE2                                  
REMARK 480     LYS G   89   CG   CD   CE   NZ                                   
REMARK 480     LEU G   91   CG   CD1  CD2                                       
REMARK 480     GLU G  123   CG   CD   OE1  OE2                                  
REMARK 480     GLN G  202   CD   OE1  NE2                                       
REMARK 480     LYS G  209   CG   CD   CE   NZ                                   
REMARK 480     GLU G  212   CB   OE1  OE2                                       
REMARK 480     LYS G  240   CD   CE   NZ                                        
REMARK 480     GLU G  241   OE1  OE2                                            
REMARK 480     GLU G  245   CG   CD   OE1  OE2                                  
REMARK 480     LYS G  247   CG   CD   CE   NZ                                   
REMARK 480     ASN G  248   CB   CG   OD1  ND2                                  
REMARK 480     LYS G  249   CG   CD   CE   NZ                                   
REMARK 480     LYS G  250   CB   CG   CD   CE   NZ                              
REMARK 480     ARG H    4   NE   CZ   NH1  NH2                                  
REMARK 480     ARG H   14   NE   CZ   NH1  NH2                                  
REMARK 480     LYS H   31   CE   NZ                                             
REMARK 480     LYS H   32   CG   CD   CE   NZ                                   
REMARK 480     GLU H   35   CG   CD   OE1  OE2                                  
REMARK 480     ILE H   50   CG2                                                 
REMARK 480     LYS H   53   CD   CE   NZ                                        
REMARK 480     LYS H   58   CE   NZ                                             
REMARK 480     LYS H   60   CD   CE   NZ                                        
REMARK 480     LYS H   89   CG   CD   CE   NZ                                   
REMARK 480     TYR H  128   CD1  CE1                                            
REMARK 480     LYS H  134   CD   CE   NZ                                        
REMARK 480     GLN H  158   CD   OE1  NE2                                       
REMARK 480     LYS H  209   CG   CD   CE   NZ                                   
REMARK 480     PHE H  232   CD1  CE1  CZ                                        
REMARK 480     GLN H  233   CG   CD   OE1  NE2                                  
REMARK 480     LYS H  240   CG   CD   CE   NZ                                   
REMARK 480     GLU H  241   OE1                                                 
REMARK 480     LYS H  247   CG   CD   CE   NZ                                   
REMARK 480     ASN H  248   CB   CG   OD1  ND2                                  
REMARK 480     LYS H  249   CG   CD   CE   NZ                                   
REMARK 480     LYS H  250   CD   CE   NZ                                        
REMARK 480     ARG H  272   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     VAL I    1   N    CA   CB                                        
REMARK 480     ARG I   14   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS I   31   CE   NZ                                             
REMARK 480     LYS I   53   CD   CE   NZ                                        
REMARK 480     LYS I   58   NZ                                                  
REMARK 480     LYS I   60   CD   CE   NZ                                        
REMARK 480     TYR I  128   CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 480     LYS I  209   CG   CD   CE   NZ                                   
REMARK 480     ARG I  272   CZ   NH1  NH2                                       
REMARK 480     ARG J    3   NE   CZ   NH1  NH2                                  
REMARK 480     ARG J    4   CD   NE   CZ   NH1  NH2                             
REMARK 480     ARG J   14   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS J   58   CB   CG   CD   CE   NZ                              
REMARK 480     LEU J   59   CG   CD1  CD2                                       
REMARK 480     LYS J   60   CE   NZ                                             
REMARK 480     LYS J   89   CG   CD   CE   NZ                                   
REMARK 480     TYR J  128   CB                                                  
REMARK 480     LYS J  209   CG   CD   CE   NZ                                   
REMARK 480     GLN J  233   CD   OE1  NE2                                       
REMARK 480     LYS J  240   CG   CD   CE   NZ                                   
REMARK 480     LYS J  247   CG   CD   CE   NZ                                   
REMARK 480     ASN J  248   CG   OD1  ND2                                       
REMARK 480     LYS J  250   CD   CE   NZ                                        
REMARK 480     ARG K    3   CB   CG   CD                                        
REMARK 480     ARG K    4   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     ARG K   14   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS K   30   CE   NZ                                             
REMARK 480     LYS K   31   CE   NZ                                             
REMARK 480     GLU K   35   CB   CG   CD   OE1  OE2                             
REMARK 480     LYS K   53   CD   CE   NZ                                        
REMARK 480     LYS K   58   CG   CD   CE   NZ                                   
REMARK 480     LYS K   76   CD   CE   NZ                                        
REMARK 480     LYS K   89   CG   CD   CE   NZ                                   
REMARK 480     GLU K   92   CG   CD   OE1  OE2                                  
REMARK 480     THR K  127   OG1  CG2                                            
REMARK 480     LYS K  134   CD   CE   NZ                                        
REMARK 480     GLN K  202   CG   CD   OE1  NE2                                  
REMARK 480     LYS K  209   CE   NZ                                             
REMARK 480     GLU K  212   CB   CG                                             
REMARK 480     ASP K  216   CG   OD1  OD2                                       
REMARK 480     LYS K  240   CD   CE   NZ                                        
REMARK 480     LYS K  247   CG   CD   CE   NZ                                   
REMARK 480     LYS K  250   CG   CD   CE   NZ                                   
REMARK 480     ARG L    4   CD   NE   CZ   NH1  NH2                             
REMARK 480     ARG L   14   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS L   31   NZ                                                  
REMARK 480     GLU L   35   CG   CD   OE1  OE2                                  
REMARK 480     LYS L   53   CD   CE   NZ                                        
REMARK 480     LYS L   58   CG   CD   CE   NZ                                   
REMARK 480     LYS L   60   CD   CE   NZ                                        
REMARK 480     LYS L   76   CE   NZ                                             
REMARK 480     LYS L   89   CD   CE   NZ                                        
REMARK 480     GLU L  123   CG   CD                                             
REMARK 480     LYS L  209   CD   CE   NZ                                        
REMARK 480     LYS L  240   CG   CD   CE   NZ                                   
REMARK 480     GLU L  245   CG   CD   OE1  OE2                                  
REMARK 480     LYS L  247   CG   CD   CE   NZ                                   
REMARK 480     ASN L  248   CG   OD1  ND2                                       
REMARK 480     LYS L  250   CG   CD   CE   NZ                                   
REMARK 480     ARG L  272   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     ARG M   14   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS M   30   CB   CG   CD   CE                                   
REMARK 480     LYS M   32   CG   CD   CE                                        
REMARK 480     GLU M   35   CB   CG   CD   OE1  OE2                             
REMARK 480     ILE M   50   CG2                                                 
REMARK 480     LYS M   53   CG   CD   CE   NZ                                   
REMARK 480     LYS M   60   CB                                                  
REMARK 480     HIS M   79   CG   ND1  CD2  CE1  NE2                             
REMARK 480     LYS M   89   CG   CD   CE   NZ                                   
REMARK 480     GLU M   92   CG   CD   OE1  OE2                                  
REMARK 480     TYR M  128   CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 480     LYS M  134   CD   CE   NZ                                        
REMARK 480     LYS M  140   CG   CD   CE   NZ                                   
REMARK 480     GLN M  202   CG   CD   OE1  NE2                                  
REMARK 480     GLU M  205   CG   CD   OE1  OE2                                  
REMARK 480     LYS M  208   CE   NZ                                             
REMARK 480     LYS M  209   CG   CD   CE   NZ                                   
REMARK 480     GLU M  212   CG   CD   OE1  OE2                                  
REMARK 480     LYS M  250   CG   CD   CE   NZ                                   
REMARK 480     ARG N    3   CB                                                  
REMARK 480     ARG N    4   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS N   32   CE   NZ                                             
REMARK 480     LYS N   53   CD   CE   NZ                                        
REMARK 480     LYS N   58   CB   CG   CD   CE   NZ                              
REMARK 480     LYS N   60   CD   CE   NZ                                        
REMARK 480     LYS N   76   CD   CE   NZ                                        
REMARK 480     LYS N   89   CG   CD   CE   NZ                                   
REMARK 480     TYR N  128   CD1  CE1  CZ   OH                                   
REMARK 480     LYS N  134   CG   CD   CE   NZ                                   
REMARK 480     LYS N  209   CD   CE   NZ                                        
REMARK 480     LYS N  240   CD   CE   NZ                                        
REMARK 480     GLN N  243   CG   CD   OE1  NE2                                  
REMARK 480     LYS N  247   CG   CD   CE   NZ                                   
REMARK 480     LYS N  250   CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ALA L 130   C   -  N   -  CA  ANGL. DEV. =  22.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  10       62.69   -108.48                                   
REMARK 500    GLU A 123      -48.03     72.85                                   
REMARK 500    TYR A 132     -117.78     51.02                                   
REMARK 500    ILE A 175      -60.83    -98.44                                   
REMARK 500    SER A 191       57.29     33.08                                   
REMARK 500    HIS A 257       48.38    -97.49                                   
REMARK 500    ALA A 271     -149.67    -92.05                                   
REMARK 500    ALA B  10       63.68   -110.10                                   
REMARK 500    GLU B 123      -32.41     71.72                                   
REMARK 500    TYR B 132     -146.63     64.92                                   
REMARK 500    LYS B 134       64.58     75.85                                   
REMARK 500    ILE B 175      -61.52    -99.04                                   
REMARK 500    SER B 191       56.60     31.59                                   
REMARK 500    HIS B 257       49.04   -104.58                                   
REMARK 500    ALA C  10       64.85   -108.88                                   
REMARK 500    GLU C 123      -39.06     86.93                                   
REMARK 500    TYR C 132     -124.83     57.17                                   
REMARK 500    ILE C 175      -63.56    -98.90                                   
REMARK 500    SER C 191       60.17     28.82                                   
REMARK 500    HIS C 257       49.94   -105.05                                   
REMARK 500    ALA C 271      -89.63    -93.75                                   
REMARK 500    ALA D  10       63.67   -109.06                                   
REMARK 500    TYR D 132     -121.20     58.41                                   
REMARK 500    SER D 191       60.88     28.40                                   
REMARK 500    HIS D 257       49.58   -105.35                                   
REMARK 500    LYS D 261     -166.30   -100.46                                   
REMARK 500    ALA D 271     -102.07    -43.25                                   
REMARK 500    ARG D 272      108.33    -47.84                                   
REMARK 500    ARG E   3      -36.19   -132.48                                   
REMARK 500    ALA E  10       64.53   -108.39                                   
REMARK 500    LYS E  32       21.27    -69.70                                   
REMARK 500    GLU E 123      -41.81     85.20                                   
REMARK 500    THR E 127      144.33   -171.52                                   
REMARK 500    MET E 131     -104.70    -62.33                                   
REMARK 500    TYR E 132      -87.78    -88.22                                   
REMARK 500    ILE E 175      -62.06    -96.87                                   
REMARK 500    SER E 191       61.30     28.18                                   
REMARK 500    HIS E 257       49.58   -106.29                                   
REMARK 500    ALA F  10       63.29   -108.20                                   
REMARK 500    GLU F 123      -50.84     84.43                                   
REMARK 500    TYR F 128       27.23     49.75                                   
REMARK 500    ALA F 129      -62.33   -147.71                                   
REMARK 500    TYR F 132     -123.08     61.42                                   
REMARK 500    ILE F 175      -60.27    -98.07                                   
REMARK 500    SER F 191       57.88     27.19                                   
REMARK 500    HIS F 257       48.96   -105.83                                   
REMARK 500    ARG G   3      -31.45   -131.91                                   
REMARK 500    ALA G  10       64.46   -110.11                                   
REMARK 500    THR G 127      148.16    166.30                                   
REMARK 500    ALA G 130       24.48    116.81                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     106 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E6A B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E6A E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD F 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD G 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD H 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E6A H 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD I 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD J 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD K 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E6A K 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD L 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD M 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E6A M 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD N 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5EA2   RELATED DB: PDB                                   
DBREF  5EAI A    0   273  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  5EAI B    0   273  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  5EAI C    0   273  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  5EAI D    0   273  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  5EAI E    0   273  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  5EAI F    0   273  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  5EAI G    0   273  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  5EAI H    0   273  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  5EAI I    0   273  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  5EAI J    0   273  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  5EAI K    0   273  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  5EAI L    0   273  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  5EAI M    0   273  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  5EAI N    0   273  UNP    P15559   NQO1_HUMAN       1    274             
SEQADV 5EAI GLY A   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI PRO A   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI HIS A   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI GLY B   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI PRO B   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI HIS B   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI GLY C   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI PRO C   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI HIS C   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI GLY D   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI PRO D   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI HIS D   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI GLY E   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI PRO E   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI HIS E   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI GLY F   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI PRO F   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI HIS F   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI GLY G   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI PRO G   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI HIS G   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI GLY H   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI PRO H   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI HIS H   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI GLY I   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI PRO I   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI HIS I   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI GLY J   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI PRO J   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI HIS J   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI GLY K   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI PRO K   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI HIS K   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI GLY L   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI PRO L   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI HIS L   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI GLY M   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI PRO M   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI HIS M   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI GLY N   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI PRO N   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 5EAI HIS N   -1  UNP  P15559              EXPRESSION TAG                 
SEQRES   1 A  277  GLY PRO HIS MET VAL GLY ARG ARG ALA LEU ILE VAL LEU          
SEQRES   2 A  277  ALA HIS SER GLU ARG THR SER PHE ASN TYR ALA MET LYS          
SEQRES   3 A  277  GLU ALA ALA ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU          
SEQRES   4 A  277  VAL VAL GLU SER ASP LEU TYR ALA MET ASN PHE ASN PRO          
SEQRES   5 A  277  ILE ILE SER ARG LYS ASP ILE THR GLY LYS LEU LYS ASP          
SEQRES   6 A  277  PRO ALA ASN PHE GLN TYR PRO ALA GLU SER VAL LEU ALA          
SEQRES   7 A  277  TYR LYS GLU GLY HIS LEU SER PRO ASP ILE VAL ALA GLU          
SEQRES   8 A  277  GLN LYS LYS LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN          
SEQRES   9 A  277  PHE PRO LEU GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS          
SEQRES  10 A  277  GLY TRP PHE GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR          
SEQRES  11 A  277  THR TYR ALA ALA MET TYR ASP LYS GLY PRO PHE ARG SER          
SEQRES  12 A  277  LYS LYS ALA VAL LEU SER ILE THR THR GLY GLY SER GLY          
SEQRES  13 A  277  SER MET TYR SER LEU GLN GLY ILE HIS GLY ASP MET ASN          
SEQRES  14 A  277  VAL ILE LEU TRP PRO ILE GLN SER GLY ILE LEU HIS PHE          
SEQRES  15 A  277  CYS GLY PHE GLN VAL LEU GLU PRO GLN LEU THR TYR SER          
SEQRES  16 A  277  ILE GLY HIS THR PRO ALA ASP ALA ARG ILE GLN ILE LEU          
SEQRES  17 A  277  GLU GLY TRP LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU          
SEQRES  18 A  277  THR PRO LEU TYR PHE ALA PRO SER SER LEU PHE ASP LEU          
SEQRES  19 A  277  ASN PHE GLN ALA GLY PHE LEU MET LYS LYS GLU VAL GLN          
SEQRES  20 A  277  ASP GLU GLU LYS ASN LYS LYS PHE GLY LEU SER VAL GLY          
SEQRES  21 A  277  HIS HIS LEU GLY LYS SER ILE PRO THR ASP ASN GLN ILE          
SEQRES  22 A  277  LYS ALA ARG LYS                                              
SEQRES   1 B  277  GLY PRO HIS MET VAL GLY ARG ARG ALA LEU ILE VAL LEU          
SEQRES   2 B  277  ALA HIS SER GLU ARG THR SER PHE ASN TYR ALA MET LYS          
SEQRES   3 B  277  GLU ALA ALA ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU          
SEQRES   4 B  277  VAL VAL GLU SER ASP LEU TYR ALA MET ASN PHE ASN PRO          
SEQRES   5 B  277  ILE ILE SER ARG LYS ASP ILE THR GLY LYS LEU LYS ASP          
SEQRES   6 B  277  PRO ALA ASN PHE GLN TYR PRO ALA GLU SER VAL LEU ALA          
SEQRES   7 B  277  TYR LYS GLU GLY HIS LEU SER PRO ASP ILE VAL ALA GLU          
SEQRES   8 B  277  GLN LYS LYS LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN          
SEQRES   9 B  277  PHE PRO LEU GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS          
SEQRES  10 B  277  GLY TRP PHE GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR          
SEQRES  11 B  277  THR TYR ALA ALA MET TYR ASP LYS GLY PRO PHE ARG SER          
SEQRES  12 B  277  LYS LYS ALA VAL LEU SER ILE THR THR GLY GLY SER GLY          
SEQRES  13 B  277  SER MET TYR SER LEU GLN GLY ILE HIS GLY ASP MET ASN          
SEQRES  14 B  277  VAL ILE LEU TRP PRO ILE GLN SER GLY ILE LEU HIS PHE          
SEQRES  15 B  277  CYS GLY PHE GLN VAL LEU GLU PRO GLN LEU THR TYR SER          
SEQRES  16 B  277  ILE GLY HIS THR PRO ALA ASP ALA ARG ILE GLN ILE LEU          
SEQRES  17 B  277  GLU GLY TRP LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU          
SEQRES  18 B  277  THR PRO LEU TYR PHE ALA PRO SER SER LEU PHE ASP LEU          
SEQRES  19 B  277  ASN PHE GLN ALA GLY PHE LEU MET LYS LYS GLU VAL GLN          
SEQRES  20 B  277  ASP GLU GLU LYS ASN LYS LYS PHE GLY LEU SER VAL GLY          
SEQRES  21 B  277  HIS HIS LEU GLY LYS SER ILE PRO THR ASP ASN GLN ILE          
SEQRES  22 B  277  LYS ALA ARG LYS                                              
SEQRES   1 C  277  GLY PRO HIS MET VAL GLY ARG ARG ALA LEU ILE VAL LEU          
SEQRES   2 C  277  ALA HIS SER GLU ARG THR SER PHE ASN TYR ALA MET LYS          
SEQRES   3 C  277  GLU ALA ALA ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU          
SEQRES   4 C  277  VAL VAL GLU SER ASP LEU TYR ALA MET ASN PHE ASN PRO          
SEQRES   5 C  277  ILE ILE SER ARG LYS ASP ILE THR GLY LYS LEU LYS ASP          
SEQRES   6 C  277  PRO ALA ASN PHE GLN TYR PRO ALA GLU SER VAL LEU ALA          
SEQRES   7 C  277  TYR LYS GLU GLY HIS LEU SER PRO ASP ILE VAL ALA GLU          
SEQRES   8 C  277  GLN LYS LYS LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN          
SEQRES   9 C  277  PHE PRO LEU GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS          
SEQRES  10 C  277  GLY TRP PHE GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR          
SEQRES  11 C  277  THR TYR ALA ALA MET TYR ASP LYS GLY PRO PHE ARG SER          
SEQRES  12 C  277  LYS LYS ALA VAL LEU SER ILE THR THR GLY GLY SER GLY          
SEQRES  13 C  277  SER MET TYR SER LEU GLN GLY ILE HIS GLY ASP MET ASN          
SEQRES  14 C  277  VAL ILE LEU TRP PRO ILE GLN SER GLY ILE LEU HIS PHE          
SEQRES  15 C  277  CYS GLY PHE GLN VAL LEU GLU PRO GLN LEU THR TYR SER          
SEQRES  16 C  277  ILE GLY HIS THR PRO ALA ASP ALA ARG ILE GLN ILE LEU          
SEQRES  17 C  277  GLU GLY TRP LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU          
SEQRES  18 C  277  THR PRO LEU TYR PHE ALA PRO SER SER LEU PHE ASP LEU          
SEQRES  19 C  277  ASN PHE GLN ALA GLY PHE LEU MET LYS LYS GLU VAL GLN          
SEQRES  20 C  277  ASP GLU GLU LYS ASN LYS LYS PHE GLY LEU SER VAL GLY          
SEQRES  21 C  277  HIS HIS LEU GLY LYS SER ILE PRO THR ASP ASN GLN ILE          
SEQRES  22 C  277  LYS ALA ARG LYS                                              
SEQRES   1 D  277  GLY PRO HIS MET VAL GLY ARG ARG ALA LEU ILE VAL LEU          
SEQRES   2 D  277  ALA HIS SER GLU ARG THR SER PHE ASN TYR ALA MET LYS          
SEQRES   3 D  277  GLU ALA ALA ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU          
SEQRES   4 D  277  VAL VAL GLU SER ASP LEU TYR ALA MET ASN PHE ASN PRO          
SEQRES   5 D  277  ILE ILE SER ARG LYS ASP ILE THR GLY LYS LEU LYS ASP          
SEQRES   6 D  277  PRO ALA ASN PHE GLN TYR PRO ALA GLU SER VAL LEU ALA          
SEQRES   7 D  277  TYR LYS GLU GLY HIS LEU SER PRO ASP ILE VAL ALA GLU          
SEQRES   8 D  277  GLN LYS LYS LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN          
SEQRES   9 D  277  PHE PRO LEU GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS          
SEQRES  10 D  277  GLY TRP PHE GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR          
SEQRES  11 D  277  THR TYR ALA ALA MET TYR ASP LYS GLY PRO PHE ARG SER          
SEQRES  12 D  277  LYS LYS ALA VAL LEU SER ILE THR THR GLY GLY SER GLY          
SEQRES  13 D  277  SER MET TYR SER LEU GLN GLY ILE HIS GLY ASP MET ASN          
SEQRES  14 D  277  VAL ILE LEU TRP PRO ILE GLN SER GLY ILE LEU HIS PHE          
SEQRES  15 D  277  CYS GLY PHE GLN VAL LEU GLU PRO GLN LEU THR TYR SER          
SEQRES  16 D  277  ILE GLY HIS THR PRO ALA ASP ALA ARG ILE GLN ILE LEU          
SEQRES  17 D  277  GLU GLY TRP LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU          
SEQRES  18 D  277  THR PRO LEU TYR PHE ALA PRO SER SER LEU PHE ASP LEU          
SEQRES  19 D  277  ASN PHE GLN ALA GLY PHE LEU MET LYS LYS GLU VAL GLN          
SEQRES  20 D  277  ASP GLU GLU LYS ASN LYS LYS PHE GLY LEU SER VAL GLY          
SEQRES  21 D  277  HIS HIS LEU GLY LYS SER ILE PRO THR ASP ASN GLN ILE          
SEQRES  22 D  277  LYS ALA ARG LYS                                              
SEQRES   1 E  277  GLY PRO HIS MET VAL GLY ARG ARG ALA LEU ILE VAL LEU          
SEQRES   2 E  277  ALA HIS SER GLU ARG THR SER PHE ASN TYR ALA MET LYS          
SEQRES   3 E  277  GLU ALA ALA ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU          
SEQRES   4 E  277  VAL VAL GLU SER ASP LEU TYR ALA MET ASN PHE ASN PRO          
SEQRES   5 E  277  ILE ILE SER ARG LYS ASP ILE THR GLY LYS LEU LYS ASP          
SEQRES   6 E  277  PRO ALA ASN PHE GLN TYR PRO ALA GLU SER VAL LEU ALA          
SEQRES   7 E  277  TYR LYS GLU GLY HIS LEU SER PRO ASP ILE VAL ALA GLU          
SEQRES   8 E  277  GLN LYS LYS LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN          
SEQRES   9 E  277  PHE PRO LEU GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS          
SEQRES  10 E  277  GLY TRP PHE GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR          
SEQRES  11 E  277  THR TYR ALA ALA MET TYR ASP LYS GLY PRO PHE ARG SER          
SEQRES  12 E  277  LYS LYS ALA VAL LEU SER ILE THR THR GLY GLY SER GLY          
SEQRES  13 E  277  SER MET TYR SER LEU GLN GLY ILE HIS GLY ASP MET ASN          
SEQRES  14 E  277  VAL ILE LEU TRP PRO ILE GLN SER GLY ILE LEU HIS PHE          
SEQRES  15 E  277  CYS GLY PHE GLN VAL LEU GLU PRO GLN LEU THR TYR SER          
SEQRES  16 E  277  ILE GLY HIS THR PRO ALA ASP ALA ARG ILE GLN ILE LEU          
SEQRES  17 E  277  GLU GLY TRP LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU          
SEQRES  18 E  277  THR PRO LEU TYR PHE ALA PRO SER SER LEU PHE ASP LEU          
SEQRES  19 E  277  ASN PHE GLN ALA GLY PHE LEU MET LYS LYS GLU VAL GLN          
SEQRES  20 E  277  ASP GLU GLU LYS ASN LYS LYS PHE GLY LEU SER VAL GLY          
SEQRES  21 E  277  HIS HIS LEU GLY LYS SER ILE PRO THR ASP ASN GLN ILE          
SEQRES  22 E  277  LYS ALA ARG LYS                                              
SEQRES   1 F  277  GLY PRO HIS MET VAL GLY ARG ARG ALA LEU ILE VAL LEU          
SEQRES   2 F  277  ALA HIS SER GLU ARG THR SER PHE ASN TYR ALA MET LYS          
SEQRES   3 F  277  GLU ALA ALA ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU          
SEQRES   4 F  277  VAL VAL GLU SER ASP LEU TYR ALA MET ASN PHE ASN PRO          
SEQRES   5 F  277  ILE ILE SER ARG LYS ASP ILE THR GLY LYS LEU LYS ASP          
SEQRES   6 F  277  PRO ALA ASN PHE GLN TYR PRO ALA GLU SER VAL LEU ALA          
SEQRES   7 F  277  TYR LYS GLU GLY HIS LEU SER PRO ASP ILE VAL ALA GLU          
SEQRES   8 F  277  GLN LYS LYS LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN          
SEQRES   9 F  277  PHE PRO LEU GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS          
SEQRES  10 F  277  GLY TRP PHE GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR          
SEQRES  11 F  277  THR TYR ALA ALA MET TYR ASP LYS GLY PRO PHE ARG SER          
SEQRES  12 F  277  LYS LYS ALA VAL LEU SER ILE THR THR GLY GLY SER GLY          
SEQRES  13 F  277  SER MET TYR SER LEU GLN GLY ILE HIS GLY ASP MET ASN          
SEQRES  14 F  277  VAL ILE LEU TRP PRO ILE GLN SER GLY ILE LEU HIS PHE          
SEQRES  15 F  277  CYS GLY PHE GLN VAL LEU GLU PRO GLN LEU THR TYR SER          
SEQRES  16 F  277  ILE GLY HIS THR PRO ALA ASP ALA ARG ILE GLN ILE LEU          
SEQRES  17 F  277  GLU GLY TRP LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU          
SEQRES  18 F  277  THR PRO LEU TYR PHE ALA PRO SER SER LEU PHE ASP LEU          
SEQRES  19 F  277  ASN PHE GLN ALA GLY PHE LEU MET LYS LYS GLU VAL GLN          
SEQRES  20 F  277  ASP GLU GLU LYS ASN LYS LYS PHE GLY LEU SER VAL GLY          
SEQRES  21 F  277  HIS HIS LEU GLY LYS SER ILE PRO THR ASP ASN GLN ILE          
SEQRES  22 F  277  LYS ALA ARG LYS                                              
SEQRES   1 G  277  GLY PRO HIS MET VAL GLY ARG ARG ALA LEU ILE VAL LEU          
SEQRES   2 G  277  ALA HIS SER GLU ARG THR SER PHE ASN TYR ALA MET LYS          
SEQRES   3 G  277  GLU ALA ALA ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU          
SEQRES   4 G  277  VAL VAL GLU SER ASP LEU TYR ALA MET ASN PHE ASN PRO          
SEQRES   5 G  277  ILE ILE SER ARG LYS ASP ILE THR GLY LYS LEU LYS ASP          
SEQRES   6 G  277  PRO ALA ASN PHE GLN TYR PRO ALA GLU SER VAL LEU ALA          
SEQRES   7 G  277  TYR LYS GLU GLY HIS LEU SER PRO ASP ILE VAL ALA GLU          
SEQRES   8 G  277  GLN LYS LYS LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN          
SEQRES   9 G  277  PHE PRO LEU GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS          
SEQRES  10 G  277  GLY TRP PHE GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR          
SEQRES  11 G  277  THR TYR ALA ALA MET TYR ASP LYS GLY PRO PHE ARG SER          
SEQRES  12 G  277  LYS LYS ALA VAL LEU SER ILE THR THR GLY GLY SER GLY          
SEQRES  13 G  277  SER MET TYR SER LEU GLN GLY ILE HIS GLY ASP MET ASN          
SEQRES  14 G  277  VAL ILE LEU TRP PRO ILE GLN SER GLY ILE LEU HIS PHE          
SEQRES  15 G  277  CYS GLY PHE GLN VAL LEU GLU PRO GLN LEU THR TYR SER          
SEQRES  16 G  277  ILE GLY HIS THR PRO ALA ASP ALA ARG ILE GLN ILE LEU          
SEQRES  17 G  277  GLU GLY TRP LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU          
SEQRES  18 G  277  THR PRO LEU TYR PHE ALA PRO SER SER LEU PHE ASP LEU          
SEQRES  19 G  277  ASN PHE GLN ALA GLY PHE LEU MET LYS LYS GLU VAL GLN          
SEQRES  20 G  277  ASP GLU GLU LYS ASN LYS LYS PHE GLY LEU SER VAL GLY          
SEQRES  21 G  277  HIS HIS LEU GLY LYS SER ILE PRO THR ASP ASN GLN ILE          
SEQRES  22 G  277  LYS ALA ARG LYS                                              
SEQRES   1 H  277  GLY PRO HIS MET VAL GLY ARG ARG ALA LEU ILE VAL LEU          
SEQRES   2 H  277  ALA HIS SER GLU ARG THR SER PHE ASN TYR ALA MET LYS          
SEQRES   3 H  277  GLU ALA ALA ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU          
SEQRES   4 H  277  VAL VAL GLU SER ASP LEU TYR ALA MET ASN PHE ASN PRO          
SEQRES   5 H  277  ILE ILE SER ARG LYS ASP ILE THR GLY LYS LEU LYS ASP          
SEQRES   6 H  277  PRO ALA ASN PHE GLN TYR PRO ALA GLU SER VAL LEU ALA          
SEQRES   7 H  277  TYR LYS GLU GLY HIS LEU SER PRO ASP ILE VAL ALA GLU          
SEQRES   8 H  277  GLN LYS LYS LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN          
SEQRES   9 H  277  PHE PRO LEU GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS          
SEQRES  10 H  277  GLY TRP PHE GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR          
SEQRES  11 H  277  THR TYR ALA ALA MET TYR ASP LYS GLY PRO PHE ARG SER          
SEQRES  12 H  277  LYS LYS ALA VAL LEU SER ILE THR THR GLY GLY SER GLY          
SEQRES  13 H  277  SER MET TYR SER LEU GLN GLY ILE HIS GLY ASP MET ASN          
SEQRES  14 H  277  VAL ILE LEU TRP PRO ILE GLN SER GLY ILE LEU HIS PHE          
SEQRES  15 H  277  CYS GLY PHE GLN VAL LEU GLU PRO GLN LEU THR TYR SER          
SEQRES  16 H  277  ILE GLY HIS THR PRO ALA ASP ALA ARG ILE GLN ILE LEU          
SEQRES  17 H  277  GLU GLY TRP LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU          
SEQRES  18 H  277  THR PRO LEU TYR PHE ALA PRO SER SER LEU PHE ASP LEU          
SEQRES  19 H  277  ASN PHE GLN ALA GLY PHE LEU MET LYS LYS GLU VAL GLN          
SEQRES  20 H  277  ASP GLU GLU LYS ASN LYS LYS PHE GLY LEU SER VAL GLY          
SEQRES  21 H  277  HIS HIS LEU GLY LYS SER ILE PRO THR ASP ASN GLN ILE          
SEQRES  22 H  277  LYS ALA ARG LYS                                              
SEQRES   1 I  277  GLY PRO HIS MET VAL GLY ARG ARG ALA LEU ILE VAL LEU          
SEQRES   2 I  277  ALA HIS SER GLU ARG THR SER PHE ASN TYR ALA MET LYS          
SEQRES   3 I  277  GLU ALA ALA ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU          
SEQRES   4 I  277  VAL VAL GLU SER ASP LEU TYR ALA MET ASN PHE ASN PRO          
SEQRES   5 I  277  ILE ILE SER ARG LYS ASP ILE THR GLY LYS LEU LYS ASP          
SEQRES   6 I  277  PRO ALA ASN PHE GLN TYR PRO ALA GLU SER VAL LEU ALA          
SEQRES   7 I  277  TYR LYS GLU GLY HIS LEU SER PRO ASP ILE VAL ALA GLU          
SEQRES   8 I  277  GLN LYS LYS LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN          
SEQRES   9 I  277  PHE PRO LEU GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS          
SEQRES  10 I  277  GLY TRP PHE GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR          
SEQRES  11 I  277  THR TYR ALA ALA MET TYR ASP LYS GLY PRO PHE ARG SER          
SEQRES  12 I  277  LYS LYS ALA VAL LEU SER ILE THR THR GLY GLY SER GLY          
SEQRES  13 I  277  SER MET TYR SER LEU GLN GLY ILE HIS GLY ASP MET ASN          
SEQRES  14 I  277  VAL ILE LEU TRP PRO ILE GLN SER GLY ILE LEU HIS PHE          
SEQRES  15 I  277  CYS GLY PHE GLN VAL LEU GLU PRO GLN LEU THR TYR SER          
SEQRES  16 I  277  ILE GLY HIS THR PRO ALA ASP ALA ARG ILE GLN ILE LEU          
SEQRES  17 I  277  GLU GLY TRP LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU          
SEQRES  18 I  277  THR PRO LEU TYR PHE ALA PRO SER SER LEU PHE ASP LEU          
SEQRES  19 I  277  ASN PHE GLN ALA GLY PHE LEU MET LYS LYS GLU VAL GLN          
SEQRES  20 I  277  ASP GLU GLU LYS ASN LYS LYS PHE GLY LEU SER VAL GLY          
SEQRES  21 I  277  HIS HIS LEU GLY LYS SER ILE PRO THR ASP ASN GLN ILE          
SEQRES  22 I  277  LYS ALA ARG LYS                                              
SEQRES   1 J  277  GLY PRO HIS MET VAL GLY ARG ARG ALA LEU ILE VAL LEU          
SEQRES   2 J  277  ALA HIS SER GLU ARG THR SER PHE ASN TYR ALA MET LYS          
SEQRES   3 J  277  GLU ALA ALA ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU          
SEQRES   4 J  277  VAL VAL GLU SER ASP LEU TYR ALA MET ASN PHE ASN PRO          
SEQRES   5 J  277  ILE ILE SER ARG LYS ASP ILE THR GLY LYS LEU LYS ASP          
SEQRES   6 J  277  PRO ALA ASN PHE GLN TYR PRO ALA GLU SER VAL LEU ALA          
SEQRES   7 J  277  TYR LYS GLU GLY HIS LEU SER PRO ASP ILE VAL ALA GLU          
SEQRES   8 J  277  GLN LYS LYS LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN          
SEQRES   9 J  277  PHE PRO LEU GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS          
SEQRES  10 J  277  GLY TRP PHE GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR          
SEQRES  11 J  277  THR TYR ALA ALA MET TYR ASP LYS GLY PRO PHE ARG SER          
SEQRES  12 J  277  LYS LYS ALA VAL LEU SER ILE THR THR GLY GLY SER GLY          
SEQRES  13 J  277  SER MET TYR SER LEU GLN GLY ILE HIS GLY ASP MET ASN          
SEQRES  14 J  277  VAL ILE LEU TRP PRO ILE GLN SER GLY ILE LEU HIS PHE          
SEQRES  15 J  277  CYS GLY PHE GLN VAL LEU GLU PRO GLN LEU THR TYR SER          
SEQRES  16 J  277  ILE GLY HIS THR PRO ALA ASP ALA ARG ILE GLN ILE LEU          
SEQRES  17 J  277  GLU GLY TRP LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU          
SEQRES  18 J  277  THR PRO LEU TYR PHE ALA PRO SER SER LEU PHE ASP LEU          
SEQRES  19 J  277  ASN PHE GLN ALA GLY PHE LEU MET LYS LYS GLU VAL GLN          
SEQRES  20 J  277  ASP GLU GLU LYS ASN LYS LYS PHE GLY LEU SER VAL GLY          
SEQRES  21 J  277  HIS HIS LEU GLY LYS SER ILE PRO THR ASP ASN GLN ILE          
SEQRES  22 J  277  LYS ALA ARG LYS                                              
SEQRES   1 K  277  GLY PRO HIS MET VAL GLY ARG ARG ALA LEU ILE VAL LEU          
SEQRES   2 K  277  ALA HIS SER GLU ARG THR SER PHE ASN TYR ALA MET LYS          
SEQRES   3 K  277  GLU ALA ALA ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU          
SEQRES   4 K  277  VAL VAL GLU SER ASP LEU TYR ALA MET ASN PHE ASN PRO          
SEQRES   5 K  277  ILE ILE SER ARG LYS ASP ILE THR GLY LYS LEU LYS ASP          
SEQRES   6 K  277  PRO ALA ASN PHE GLN TYR PRO ALA GLU SER VAL LEU ALA          
SEQRES   7 K  277  TYR LYS GLU GLY HIS LEU SER PRO ASP ILE VAL ALA GLU          
SEQRES   8 K  277  GLN LYS LYS LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN          
SEQRES   9 K  277  PHE PRO LEU GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS          
SEQRES  10 K  277  GLY TRP PHE GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR          
SEQRES  11 K  277  THR TYR ALA ALA MET TYR ASP LYS GLY PRO PHE ARG SER          
SEQRES  12 K  277  LYS LYS ALA VAL LEU SER ILE THR THR GLY GLY SER GLY          
SEQRES  13 K  277  SER MET TYR SER LEU GLN GLY ILE HIS GLY ASP MET ASN          
SEQRES  14 K  277  VAL ILE LEU TRP PRO ILE GLN SER GLY ILE LEU HIS PHE          
SEQRES  15 K  277  CYS GLY PHE GLN VAL LEU GLU PRO GLN LEU THR TYR SER          
SEQRES  16 K  277  ILE GLY HIS THR PRO ALA ASP ALA ARG ILE GLN ILE LEU          
SEQRES  17 K  277  GLU GLY TRP LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU          
SEQRES  18 K  277  THR PRO LEU TYR PHE ALA PRO SER SER LEU PHE ASP LEU          
SEQRES  19 K  277  ASN PHE GLN ALA GLY PHE LEU MET LYS LYS GLU VAL GLN          
SEQRES  20 K  277  ASP GLU GLU LYS ASN LYS LYS PHE GLY LEU SER VAL GLY          
SEQRES  21 K  277  HIS HIS LEU GLY LYS SER ILE PRO THR ASP ASN GLN ILE          
SEQRES  22 K  277  LYS ALA ARG LYS                                              
SEQRES   1 L  277  GLY PRO HIS MET VAL GLY ARG ARG ALA LEU ILE VAL LEU          
SEQRES   2 L  277  ALA HIS SER GLU ARG THR SER PHE ASN TYR ALA MET LYS          
SEQRES   3 L  277  GLU ALA ALA ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU          
SEQRES   4 L  277  VAL VAL GLU SER ASP LEU TYR ALA MET ASN PHE ASN PRO          
SEQRES   5 L  277  ILE ILE SER ARG LYS ASP ILE THR GLY LYS LEU LYS ASP          
SEQRES   6 L  277  PRO ALA ASN PHE GLN TYR PRO ALA GLU SER VAL LEU ALA          
SEQRES   7 L  277  TYR LYS GLU GLY HIS LEU SER PRO ASP ILE VAL ALA GLU          
SEQRES   8 L  277  GLN LYS LYS LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN          
SEQRES   9 L  277  PHE PRO LEU GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS          
SEQRES  10 L  277  GLY TRP PHE GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR          
SEQRES  11 L  277  THR TYR ALA ALA MET TYR ASP LYS GLY PRO PHE ARG SER          
SEQRES  12 L  277  LYS LYS ALA VAL LEU SER ILE THR THR GLY GLY SER GLY          
SEQRES  13 L  277  SER MET TYR SER LEU GLN GLY ILE HIS GLY ASP MET ASN          
SEQRES  14 L  277  VAL ILE LEU TRP PRO ILE GLN SER GLY ILE LEU HIS PHE          
SEQRES  15 L  277  CYS GLY PHE GLN VAL LEU GLU PRO GLN LEU THR TYR SER          
SEQRES  16 L  277  ILE GLY HIS THR PRO ALA ASP ALA ARG ILE GLN ILE LEU          
SEQRES  17 L  277  GLU GLY TRP LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU          
SEQRES  18 L  277  THR PRO LEU TYR PHE ALA PRO SER SER LEU PHE ASP LEU          
SEQRES  19 L  277  ASN PHE GLN ALA GLY PHE LEU MET LYS LYS GLU VAL GLN          
SEQRES  20 L  277  ASP GLU GLU LYS ASN LYS LYS PHE GLY LEU SER VAL GLY          
SEQRES  21 L  277  HIS HIS LEU GLY LYS SER ILE PRO THR ASP ASN GLN ILE          
SEQRES  22 L  277  LYS ALA ARG LYS                                              
SEQRES   1 M  277  GLY PRO HIS MET VAL GLY ARG ARG ALA LEU ILE VAL LEU          
SEQRES   2 M  277  ALA HIS SER GLU ARG THR SER PHE ASN TYR ALA MET LYS          
SEQRES   3 M  277  GLU ALA ALA ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU          
SEQRES   4 M  277  VAL VAL GLU SER ASP LEU TYR ALA MET ASN PHE ASN PRO          
SEQRES   5 M  277  ILE ILE SER ARG LYS ASP ILE THR GLY LYS LEU LYS ASP          
SEQRES   6 M  277  PRO ALA ASN PHE GLN TYR PRO ALA GLU SER VAL LEU ALA          
SEQRES   7 M  277  TYR LYS GLU GLY HIS LEU SER PRO ASP ILE VAL ALA GLU          
SEQRES   8 M  277  GLN LYS LYS LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN          
SEQRES   9 M  277  PHE PRO LEU GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS          
SEQRES  10 M  277  GLY TRP PHE GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR          
SEQRES  11 M  277  THR TYR ALA ALA MET TYR ASP LYS GLY PRO PHE ARG SER          
SEQRES  12 M  277  LYS LYS ALA VAL LEU SER ILE THR THR GLY GLY SER GLY          
SEQRES  13 M  277  SER MET TYR SER LEU GLN GLY ILE HIS GLY ASP MET ASN          
SEQRES  14 M  277  VAL ILE LEU TRP PRO ILE GLN SER GLY ILE LEU HIS PHE          
SEQRES  15 M  277  CYS GLY PHE GLN VAL LEU GLU PRO GLN LEU THR TYR SER          
SEQRES  16 M  277  ILE GLY HIS THR PRO ALA ASP ALA ARG ILE GLN ILE LEU          
SEQRES  17 M  277  GLU GLY TRP LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU          
SEQRES  18 M  277  THR PRO LEU TYR PHE ALA PRO SER SER LEU PHE ASP LEU          
SEQRES  19 M  277  ASN PHE GLN ALA GLY PHE LEU MET LYS LYS GLU VAL GLN          
SEQRES  20 M  277  ASP GLU GLU LYS ASN LYS LYS PHE GLY LEU SER VAL GLY          
SEQRES  21 M  277  HIS HIS LEU GLY LYS SER ILE PRO THR ASP ASN GLN ILE          
SEQRES  22 M  277  LYS ALA ARG LYS                                              
SEQRES   1 N  277  GLY PRO HIS MET VAL GLY ARG ARG ALA LEU ILE VAL LEU          
SEQRES   2 N  277  ALA HIS SER GLU ARG THR SER PHE ASN TYR ALA MET LYS          
SEQRES   3 N  277  GLU ALA ALA ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU          
SEQRES   4 N  277  VAL VAL GLU SER ASP LEU TYR ALA MET ASN PHE ASN PRO          
SEQRES   5 N  277  ILE ILE SER ARG LYS ASP ILE THR GLY LYS LEU LYS ASP          
SEQRES   6 N  277  PRO ALA ASN PHE GLN TYR PRO ALA GLU SER VAL LEU ALA          
SEQRES   7 N  277  TYR LYS GLU GLY HIS LEU SER PRO ASP ILE VAL ALA GLU          
SEQRES   8 N  277  GLN LYS LYS LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN          
SEQRES   9 N  277  PHE PRO LEU GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS          
SEQRES  10 N  277  GLY TRP PHE GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR          
SEQRES  11 N  277  THR TYR ALA ALA MET TYR ASP LYS GLY PRO PHE ARG SER          
SEQRES  12 N  277  LYS LYS ALA VAL LEU SER ILE THR THR GLY GLY SER GLY          
SEQRES  13 N  277  SER MET TYR SER LEU GLN GLY ILE HIS GLY ASP MET ASN          
SEQRES  14 N  277  VAL ILE LEU TRP PRO ILE GLN SER GLY ILE LEU HIS PHE          
SEQRES  15 N  277  CYS GLY PHE GLN VAL LEU GLU PRO GLN LEU THR TYR SER          
SEQRES  16 N  277  ILE GLY HIS THR PRO ALA ASP ALA ARG ILE GLN ILE LEU          
SEQRES  17 N  277  GLU GLY TRP LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU          
SEQRES  18 N  277  THR PRO LEU TYR PHE ALA PRO SER SER LEU PHE ASP LEU          
SEQRES  19 N  277  ASN PHE GLN ALA GLY PHE LEU MET LYS LYS GLU VAL GLN          
SEQRES  20 N  277  ASP GLU GLU LYS ASN LYS LYS PHE GLY LEU SER VAL GLY          
SEQRES  21 N  277  HIS HIS LEU GLY LYS SER ILE PRO THR ASP ASN GLN ILE          
SEQRES  22 N  277  LYS ALA ARG LYS                                              
HET    FAD  A 601      53                                                       
HET    FAD  B 301      53                                                       
HET    E6A  B 302      26                                                       
HET    FAD  C 601      53                                                       
HET    FAD  D 301      53                                                       
HET    FAD  E 601      53                                                       
HET    E6A  E 602      26                                                       
HET    FAD  F 301      53                                                       
HET    FAD  G 601      53                                                       
HET    FAD  H 301      53                                                       
HET    E6A  H 302      26                                                       
HET    FAD  I 601      53                                                       
HET    FAD  J 301      53                                                       
HET    FAD  K 601      53                                                       
HET    E6A  K 602      26                                                       
HET    FAD  L 301      53                                                       
HET    FAD  M 601      53                                                       
HET    E6A  M 602      26                                                       
HET    FAD  N 301      53                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     E6A (2~{R},3~{R})-2-[(2~{S},3~{S})-3-BROMANYL-1,4-                   
HETNAM   2 E6A  BIS(OXIDANYLIDENE)-2,3-DIHYDRONAPHTHALEN-2-YL]-3-               
HETNAM   3 E6A  OXIDANYL-2,3-DIHYDRONAPHTHALENE-1,4-DIONE                       
FORMUL  15  FAD    14(C27 H33 N9 O15 P2)                                        
FORMUL  17  E6A    5(C20 H13 BR O5)                                             
FORMUL  34  HOH   *50(H2 O)                                                     
HELIX    1 AA1 SER A   16  LYS A   32  1                                  17    
HELIX    2 AA2 SER A   51  ILE A   55  5                                   5    
HELIX    3 AA3 GLN A   66  GLU A   77  1                                  12    
HELIX    4 AA4 SER A   81  ALA A   94  1                                  14    
HELIX    5 AA5 PRO A  109  PHE A  120  1                                  12    
HELIX    6 AA6 MET A  131  GLY A  135  5                                   5    
HELIX    7 AA7 SER A  151  SER A  156  5                                   6    
HELIX    8 AA8 ASP A  163  SER A  173  1                                  11    
HELIX    9 AA9 LEU A  176  GLY A  180  5                                   5    
HELIX   10 AB1 SER A  191  THR A  195  5                                   5    
HELIX   11 AB2 PRO A  196  GLU A  212  1                                  17    
HELIX   12 AB3 ASN A  213  GLU A  217  5                                   5    
HELIX   13 AB4 PRO A  224  PHE A  228  5                                   5    
HELIX   14 AB5 ASN A  231  GLY A  235  5                                   5    
HELIX   15 AB6 LYS A  239  ASN A  248  1                                  10    
HELIX   16 AB7 SER B   16  LYS B   32  1                                  17    
HELIX   17 AB8 SER B   51  ILE B   55  5                                   5    
HELIX   18 AB9 GLN B   66  GLU B   77  1                                  12    
HELIX   19 AC1 SER B   81  ALA B   94  1                                  14    
HELIX   20 AC2 PRO B  109  PHE B  120  1                                  12    
HELIX   21 AC3 SER B  151  SER B  156  5                                   6    
HELIX   22 AC4 ASP B  163  SER B  173  1                                  11    
HELIX   23 AC5 LEU B  176  GLY B  180  5                                   5    
HELIX   24 AC6 PRO B  196  GLU B  212  1                                  17    
HELIX   25 AC7 PRO B  224  PHE B  228  5                                   5    
HELIX   26 AC8 LYS B  239  GLU B  246  1                                   8    
HELIX   27 AC9 SER C   16  LYS C   32  1                                  17    
HELIX   28 AD1 SER C   51  ILE C   55  5                                   5    
HELIX   29 AD2 GLN C   66  GLY C   78  1                                  13    
HELIX   30 AD3 SER C   81  ALA C   94  1                                  14    
HELIX   31 AD4 PRO C  109  PHE C  120  1                                  12    
HELIX   32 AD5 MET C  131  GLY C  135  5                                   5    
HELIX   33 AD6 SER C  151  SER C  156  5                                   6    
HELIX   34 AD7 ASP C  163  SER C  173  1                                  11    
HELIX   35 AD8 LEU C  176  GLY C  180  5                                   5    
HELIX   36 AD9 SER C  191  THR C  195  5                                   5    
HELIX   37 AE1 PRO C  196  GLU C  212  1                                  17    
HELIX   38 AE2 PRO C  224  PHE C  228  5                                   5    
HELIX   39 AE3 ASN C  231  GLY C  235  5                                   5    
HELIX   40 AE4 LYS C  239  LYS C  247  1                                   9    
HELIX   41 AE5 SER D   16  LYS D   32  1                                  17    
HELIX   42 AE6 SER D   51  ILE D   55  5                                   5    
HELIX   43 AE7 GLN D   66  GLY D   78  1                                  13    
HELIX   44 AE8 SER D   81  ALA D   94  1                                  14    
HELIX   45 AE9 PRO D  109  PHE D  120  1                                  12    
HELIX   46 AF1 MET D  131  GLY D  135  5                                   5    
HELIX   47 AF2 SER D  151  SER D  156  5                                   6    
HELIX   48 AF3 ASP D  163  SER D  173  1                                  11    
HELIX   49 AF4 LEU D  176  GLY D  180  5                                   5    
HELIX   50 AF5 SER D  191  THR D  195  5                                   5    
HELIX   51 AF6 PRO D  196  GLU D  212  1                                  17    
HELIX   52 AF7 PRO D  224  PHE D  228  5                                   5    
HELIX   53 AF8 LYS D  239  ASN D  248  1                                  10    
HELIX   54 AF9 SER E   16  LYS E   32  1                                  17    
HELIX   55 AG1 SER E   51  ILE E   55  5                                   5    
HELIX   56 AG2 GLN E   66  GLU E   77  1                                  12    
HELIX   57 AG3 SER E   81  ALA E   94  1                                  14    
HELIX   58 AG4 PRO E  109  PHE E  120  1                                  12    
HELIX   59 AG5 SER E  151  SER E  156  5                                   6    
HELIX   60 AG6 ASP E  163  SER E  173  1                                  11    
HELIX   61 AG7 LEU E  176  GLY E  180  5                                   5    
HELIX   62 AG8 PRO E  196  GLU E  212  1                                  17    
HELIX   63 AG9 PRO E  224  PHE E  228  5                                   5    
HELIX   64 AH1 LYS E  239  LYS E  247  1                                   9    
HELIX   65 AH2 SER F   16  LYS F   32  1                                  17    
HELIX   66 AH3 SER F   51  ILE F   55  5                                   5    
HELIX   67 AH4 GLN F   66  GLY F   78  1                                  13    
HELIX   68 AH5 SER F   81  ALA F   94  1                                  14    
HELIX   69 AH6 PRO F  109  PHE F  120  1                                  12    
HELIX   70 AH7 MET F  131  GLY F  135  5                                   5    
HELIX   71 AH8 SER F  151  SER F  156  5                                   6    
HELIX   72 AH9 ASP F  163  SER F  173  1                                  11    
HELIX   73 AI1 LEU F  176  GLY F  180  5                                   5    
HELIX   74 AI2 PRO F  196  GLU F  212  1                                  17    
HELIX   75 AI3 PRO F  224  PHE F  228  5                                   5    
HELIX   76 AI4 ASN F  231  GLY F  235  5                                   5    
HELIX   77 AI5 LYS F  239  LYS F  247  1                                   9    
HELIX   78 AI6 SER G   16  LYS G   32  1                                  17    
HELIX   79 AI7 SER G   51  ILE G   55  5                                   5    
HELIX   80 AI8 GLN G   66  GLU G   77  1                                  12    
HELIX   81 AI9 SER G   81  ALA G   94  1                                  14    
HELIX   82 AJ1 PRO G  109  PHE G  120  1                                  12    
HELIX   83 AJ2 ILE G  121  TYR G  126  1                                   6    
HELIX   84 AJ3 MET G  131  GLY G  135  5                                   5    
HELIX   85 AJ4 SER G  151  SER G  156  5                                   6    
HELIX   86 AJ5 ASP G  163  SER G  173  1                                  11    
HELIX   87 AJ6 LEU G  176  GLY G  180  5                                   5    
HELIX   88 AJ7 PRO G  196  GLU G  212  1                                  17    
HELIX   89 AJ8 PRO G  224  PHE G  228  5                                   5    
HELIX   90 AJ9 LYS G  239  LYS G  247  1                                   9    
HELIX   91 AK1 SER H   16  LYS H   32  1                                  17    
HELIX   92 AK2 SER H   51  ILE H   55  5                                   5    
HELIX   93 AK3 GLN H   66  GLY H   78  1                                  13    
HELIX   94 AK4 SER H   81  ALA H   94  1                                  14    
HELIX   95 AK5 PRO H  109  PHE H  120  1                                  12    
HELIX   96 AK6 ILE H  121  TYR H  126  1                                   6    
HELIX   97 AK7 MET H  131  GLY H  135  5                                   5    
HELIX   98 AK8 SER H  151  SER H  156  5                                   6    
HELIX   99 AK9 ASP H  163  SER H  173  1                                  11    
HELIX  100 AL1 LEU H  176  GLY H  180  5                                   5    
HELIX  101 AL2 SER H  191  THR H  195  5                                   5    
HELIX  102 AL3 PRO H  196  GLU H  212  1                                  17    
HELIX  103 AL4 PRO H  224  PHE H  228  5                                   5    
HELIX  104 AL5 ASN H  231  GLY H  235  5                                   5    
HELIX  105 AL6 LYS H  239  GLU H  246  1                                   8    
HELIX  106 AL7 SER I   16  LYS I   32  1                                  17    
HELIX  107 AL8 SER I   51  ILE I   55  5                                   5    
HELIX  108 AL9 GLN I   66  GLY I   78  1                                  13    
HELIX  109 AM1 SER I   81  ALA I   94  1                                  14    
HELIX  110 AM2 PRO I  109  PHE I  120  1                                  12    
HELIX  111 AM3 ILE I  121  TYR I  126  1                                   6    
HELIX  112 AM4 MET I  131  GLY I  135  5                                   5    
HELIX  113 AM5 SER I  151  SER I  156  5                                   6    
HELIX  114 AM6 ASP I  163  SER I  173  1                                  11    
HELIX  115 AM7 LEU I  176  GLY I  180  5                                   5    
HELIX  116 AM8 PRO I  196  GLU I  212  1                                  17    
HELIX  117 AM9 PRO I  224  PHE I  228  5                                   5    
HELIX  118 AN1 LYS I  239  LYS I  247  1                                   9    
HELIX  119 AN2 SER J   16  LYS J   32  1                                  17    
HELIX  120 AN3 SER J   51  ILE J   55  5                                   5    
HELIX  121 AN4 GLN J   66  GLU J   77  1                                  12    
HELIX  122 AN5 SER J   81  ALA J   94  1                                  14    
HELIX  123 AN6 PRO J  109  PHE J  120  1                                  12    
HELIX  124 AN7 MET J  131  GLY J  135  5                                   5    
HELIX  125 AN8 SER J  151  SER J  156  5                                   6    
HELIX  126 AN9 ASP J  163  SER J  173  1                                  11    
HELIX  127 AO1 LEU J  176  GLY J  180  5                                   5    
HELIX  128 AO2 SER J  191  THR J  195  5                                   5    
HELIX  129 AO3 PRO J  196  GLU J  212  1                                  17    
HELIX  130 AO4 PRO J  224  PHE J  228  5                                   5    
HELIX  131 AO5 LYS J  239  LYS J  247  1                                   9    
HELIX  132 AO6 SER K   16  LYS K   32  1                                  17    
HELIX  133 AO7 SER K   51  ILE K   55  5                                   5    
HELIX  134 AO8 GLN K   66  GLY K   78  1                                  13    
HELIX  135 AO9 SER K   81  ALA K   94  1                                  14    
HELIX  136 AP1 PRO K  109  PHE K  120  1                                  12    
HELIX  137 AP2 ILE K  121  TYR K  126  1                                   6    
HELIX  138 AP3 MET K  131  GLY K  135  5                                   5    
HELIX  139 AP4 SER K  151  SER K  156  5                                   6    
HELIX  140 AP5 ASP K  163  SER K  173  1                                  11    
HELIX  141 AP6 LEU K  176  GLY K  180  5                                   5    
HELIX  142 AP7 SER K  191  THR K  195  5                                   5    
HELIX  143 AP8 PRO K  196  GLU K  212  1                                  17    
HELIX  144 AP9 PRO K  224  PHE K  228  5                                   5    
HELIX  145 AQ1 LYS K  239  LYS K  247  1                                   9    
HELIX  146 AQ2 SER L   16  LYS L   32  1                                  17    
HELIX  147 AQ3 SER L   51  ILE L   55  5                                   5    
HELIX  148 AQ4 GLN L   66  GLY L   78  1                                  13    
HELIX  149 AQ5 SER L   81  ALA L   94  1                                  14    
HELIX  150 AQ6 PRO L  109  PHE L  120  1                                  12    
HELIX  151 AQ7 ILE L  121  TYR L  126  1                                   6    
HELIX  152 AQ8 MET L  131  GLY L  135  5                                   5    
HELIX  153 AQ9 SER L  151  SER L  156  5                                   6    
HELIX  154 AR1 ASP L  163  SER L  173  1                                  11    
HELIX  155 AR2 LEU L  176  GLY L  180  5                                   5    
HELIX  156 AR3 PRO L  196  GLU L  212  1                                  17    
HELIX  157 AR4 PRO L  224  PHE L  228  5                                   5    
HELIX  158 AR5 ASN L  231  GLY L  235  5                                   5    
HELIX  159 AR6 LYS L  239  ASN L  248  1                                  10    
HELIX  160 AR7 SER M   16  LYS M   32  1                                  17    
HELIX  161 AR8 SER M   51  ILE M   55  5                                   5    
HELIX  162 AR9 GLN M   66  GLY M   78  1                                  13    
HELIX  163 AS1 SER M   81  ALA M   94  1                                  14    
HELIX  164 AS2 PRO M  109  PHE M  120  1                                  12    
HELIX  165 AS3 ILE M  121  TYR M  126  1                                   6    
HELIX  166 AS4 MET M  131  GLY M  135  5                                   5    
HELIX  167 AS5 SER M  151  SER M  156  5                                   6    
HELIX  168 AS6 ASP M  163  SER M  173  1                                  11    
HELIX  169 AS7 LEU M  176  GLY M  180  5                                   5    
HELIX  170 AS8 PRO M  196  GLU M  212  1                                  17    
HELIX  171 AS9 PRO M  224  PHE M  228  5                                   5    
HELIX  172 AT1 LYS M  239  GLU M  246  1                                   8    
HELIX  173 AT2 SER N   16  LYS N   32  1                                  17    
HELIX  174 AT3 SER N   51  ILE N   55  5                                   5    
HELIX  175 AT4 GLN N   66  GLU N   77  1                                  12    
HELIX  176 AT5 SER N   81  ALA N   94  1                                  14    
HELIX  177 AT6 PRO N  109  PHE N  120  1                                  12    
HELIX  178 AT7 MET N  131  GLY N  135  5                                   5    
HELIX  179 AT8 SER N  151  SER N  156  5                                   6    
HELIX  180 AT9 ASP N  163  SER N  173  1                                  11    
HELIX  181 AU1 LEU N  176  GLY N  180  5                                   5    
HELIX  182 AU2 PRO N  196  GLU N  212  1                                  17    
HELIX  183 AU3 PRO N  224  PHE N  228  5                                   5    
HELIX  184 AU4 ASN N  231  GLY N  235  5                                   5    
HELIX  185 AU5 LYS N  239  LYS N  247  1                                   9    
SHEET    1 AA1 5 GLU A  35  ASP A  40  0                                        
SHEET    2 AA1 5 ARG A   4  LEU A   9  1  N  ALA A   5   O  GLU A  35           
SHEET    3 AA1 5 LEU A  96  PRO A 102  1  O  ILE A  98   N  VAL A   8           
SHEET    4 AA1 5 LYS A 141  THR A 147  1  O  SER A 145   N  PHE A  99           
SHEET    5 AA1 5 GLN A 182  VAL A 183  1  O  GLN A 182   N  ALA A 142           
SHEET    1 AA2 5 GLU A  35  ASP A  40  0                                        
SHEET    2 AA2 5 ARG A   4  LEU A   9  1  N  ALA A   5   O  GLU A  35           
SHEET    3 AA2 5 LEU A  96  PRO A 102  1  O  ILE A  98   N  VAL A   8           
SHEET    4 AA2 5 LYS A 141  THR A 147  1  O  SER A 145   N  PHE A  99           
SHEET    5 AA2 5 GLN A 187  THR A 189  1  O  GLN A 187   N  LEU A 144           
SHEET    1 AA3 5 GLU B  35  ASP B  40  0                                        
SHEET    2 AA3 5 ARG B   4  LEU B   9  1  N  ALA B   5   O  GLU B  35           
SHEET    3 AA3 5 LEU B  96  PRO B 102  1  O  ILE B  98   N  VAL B   8           
SHEET    4 AA3 5 LYS B 141  THR B 147  1  O  SER B 145   N  PHE B  99           
SHEET    5 AA3 5 GLN B 182  VAL B 183  1  O  GLN B 182   N  ALA B 142           
SHEET    1 AA4 5 GLU B  35  ASP B  40  0                                        
SHEET    2 AA4 5 ARG B   4  LEU B   9  1  N  ALA B   5   O  GLU B  35           
SHEET    3 AA4 5 LEU B  96  PRO B 102  1  O  ILE B  98   N  VAL B   8           
SHEET    4 AA4 5 LYS B 141  THR B 147  1  O  SER B 145   N  PHE B  99           
SHEET    5 AA4 5 GLN B 187  THR B 189  1  O  GLN B 187   N  LEU B 144           
SHEET    1 AA5 5 GLU C  35  ASP C  40  0                                        
SHEET    2 AA5 5 ARG C   4  LEU C   9  1  N  ALA C   5   O  GLU C  35           
SHEET    3 AA5 5 LEU C  96  PRO C 102  1  O  ILE C  98   N  VAL C   8           
SHEET    4 AA5 5 LYS C 141  THR C 147  1  O  SER C 145   N  PHE C  99           
SHEET    5 AA5 5 GLN C 182  VAL C 183  1  O  GLN C 182   N  ALA C 142           
SHEET    1 AA6 5 GLU C  35  ASP C  40  0                                        
SHEET    2 AA6 5 ARG C   4  LEU C   9  1  N  ALA C   5   O  GLU C  35           
SHEET    3 AA6 5 LEU C  96  PRO C 102  1  O  ILE C  98   N  VAL C   8           
SHEET    4 AA6 5 LYS C 141  THR C 147  1  O  SER C 145   N  PHE C  99           
SHEET    5 AA6 5 GLN C 187  THR C 189  1  O  THR C 189   N  ILE C 146           
SHEET    1 AA7 5 GLU D  35  ASP D  40  0                                        
SHEET    2 AA7 5 ARG D   4  LEU D   9  1  N  ALA D   5   O  GLU D  35           
SHEET    3 AA7 5 LEU D  96  PRO D 102  1  O  ILE D  98   N  VAL D   8           
SHEET    4 AA7 5 LYS D 141  THR D 147  1  O  SER D 145   N  PHE D  99           
SHEET    5 AA7 5 GLN D 182  VAL D 183  1  O  GLN D 182   N  ALA D 142           
SHEET    1 AA8 5 GLU D  35  ASP D  40  0                                        
SHEET    2 AA8 5 ARG D   4  LEU D   9  1  N  ALA D   5   O  GLU D  35           
SHEET    3 AA8 5 LEU D  96  PRO D 102  1  O  ILE D  98   N  VAL D   8           
SHEET    4 AA8 5 LYS D 141  THR D 147  1  O  SER D 145   N  PHE D  99           
SHEET    5 AA8 5 GLN D 187  THR D 189  1  O  GLN D 187   N  LEU D 144           
SHEET    1 AA9 5 GLU E  35  ASP E  40  0                                        
SHEET    2 AA9 5 ARG E   4  LEU E   9  1  N  ALA E   5   O  GLU E  35           
SHEET    3 AA9 5 LEU E  96  PRO E 102  1  O  ILE E  98   N  VAL E   8           
SHEET    4 AA9 5 LYS E 141  THR E 147  1  O  SER E 145   N  PHE E  99           
SHEET    5 AA9 5 GLN E 182  VAL E 183  1  O  GLN E 182   N  ALA E 142           
SHEET    1 AB1 5 GLU E  35  ASP E  40  0                                        
SHEET    2 AB1 5 ARG E   4  LEU E   9  1  N  ALA E   5   O  GLU E  35           
SHEET    3 AB1 5 LEU E  96  PRO E 102  1  O  ILE E  98   N  VAL E   8           
SHEET    4 AB1 5 LYS E 141  THR E 147  1  O  SER E 145   N  PHE E  99           
SHEET    5 AB1 5 GLN E 187  THR E 189  1  O  GLN E 187   N  LEU E 144           
SHEET    1 AB2 5 GLU F  35  ASP F  40  0                                        
SHEET    2 AB2 5 ARG F   4  LEU F   9  1  N  ALA F   5   O  GLU F  35           
SHEET    3 AB2 5 LEU F  96  PRO F 102  1  O  ILE F  98   N  VAL F   8           
SHEET    4 AB2 5 LYS F 141  THR F 147  1  O  SER F 145   N  PHE F  99           
SHEET    5 AB2 5 GLN F 182  VAL F 183  1  O  GLN F 182   N  ALA F 142           
SHEET    1 AB3 5 GLU F  35  ASP F  40  0                                        
SHEET    2 AB3 5 ARG F   4  LEU F   9  1  N  ALA F   5   O  GLU F  35           
SHEET    3 AB3 5 LEU F  96  PRO F 102  1  O  ILE F  98   N  VAL F   8           
SHEET    4 AB3 5 LYS F 141  THR F 147  1  O  SER F 145   N  PHE F  99           
SHEET    5 AB3 5 GLN F 187  THR F 189  1  O  GLN F 187   N  LEU F 144           
SHEET    1 AB4 5 GLU G  35  ASP G  40  0                                        
SHEET    2 AB4 5 ARG G   4  LEU G   9  1  N  ALA G   5   O  GLU G  35           
SHEET    3 AB4 5 LEU G  96  PRO G 102  1  O  ILE G  98   N  LEU G   6           
SHEET    4 AB4 5 LYS G 141  THR G 147  1  O  SER G 145   N  PHE G  99           
SHEET    5 AB4 5 GLN G 182  VAL G 183  1  O  GLN G 182   N  ALA G 142           
SHEET    1 AB5 5 GLU G  35  ASP G  40  0                                        
SHEET    2 AB5 5 ARG G   4  LEU G   9  1  N  ALA G   5   O  GLU G  35           
SHEET    3 AB5 5 LEU G  96  PRO G 102  1  O  ILE G  98   N  LEU G   6           
SHEET    4 AB5 5 LYS G 141  THR G 147  1  O  SER G 145   N  PHE G  99           
SHEET    5 AB5 5 GLN G 187  THR G 189  1  O  GLN G 187   N  LEU G 144           
SHEET    1 AB6 5 GLU H  35  ASP H  40  0                                        
SHEET    2 AB6 5 ARG H   4  LEU H   9  1  N  ALA H   5   O  GLU H  35           
SHEET    3 AB6 5 LEU H  96  PRO H 102  1  O  ILE H  98   N  VAL H   8           
SHEET    4 AB6 5 LYS H 141  THR H 147  1  O  SER H 145   N  PHE H  99           
SHEET    5 AB6 5 GLN H 182  VAL H 183  1  O  GLN H 182   N  ALA H 142           
SHEET    1 AB7 5 GLU H  35  ASP H  40  0                                        
SHEET    2 AB7 5 ARG H   4  LEU H   9  1  N  ALA H   5   O  GLU H  35           
SHEET    3 AB7 5 LEU H  96  PRO H 102  1  O  ILE H  98   N  VAL H   8           
SHEET    4 AB7 5 LYS H 141  THR H 147  1  O  SER H 145   N  PHE H  99           
SHEET    5 AB7 5 GLN H 187  THR H 189  1  O  GLN H 187   N  LEU H 144           
SHEET    1 AB8 5 GLU I  35  ASP I  40  0                                        
SHEET    2 AB8 5 ARG I   4  LEU I   9  1  N  ALA I   5   O  GLU I  35           
SHEET    3 AB8 5 LEU I  96  PRO I 102  1  O  ILE I  98   N  VAL I   8           
SHEET    4 AB8 5 LYS I 141  THR I 147  1  O  SER I 145   N  PHE I  99           
SHEET    5 AB8 5 GLN I 182  VAL I 183  1  O  GLN I 182   N  ALA I 142           
SHEET    1 AB9 5 GLU I  35  ASP I  40  0                                        
SHEET    2 AB9 5 ARG I   4  LEU I   9  1  N  ALA I   5   O  GLU I  35           
SHEET    3 AB9 5 LEU I  96  PRO I 102  1  O  ILE I  98   N  VAL I   8           
SHEET    4 AB9 5 LYS I 141  THR I 147  1  O  SER I 145   N  PHE I  99           
SHEET    5 AB9 5 GLN I 187  THR I 189  1  O  GLN I 187   N  LEU I 144           
SHEET    1 AC1 5 GLU J  35  ASP J  40  0                                        
SHEET    2 AC1 5 ARG J   4  LEU J   9  1  N  ALA J   5   O  GLU J  35           
SHEET    3 AC1 5 LEU J  96  PRO J 102  1  O  ILE J  98   N  VAL J   8           
SHEET    4 AC1 5 LYS J 141  THR J 147  1  O  SER J 145   N  PHE J  99           
SHEET    5 AC1 5 GLN J 182  VAL J 183  1  O  GLN J 182   N  ALA J 142           
SHEET    1 AC2 5 GLU J  35  ASP J  40  0                                        
SHEET    2 AC2 5 ARG J   4  LEU J   9  1  N  ALA J   5   O  GLU J  35           
SHEET    3 AC2 5 LEU J  96  PRO J 102  1  O  ILE J  98   N  VAL J   8           
SHEET    4 AC2 5 LYS J 141  THR J 147  1  O  SER J 145   N  PHE J  99           
SHEET    5 AC2 5 GLN J 187  THR J 189  1  O  GLN J 187   N  LEU J 144           
SHEET    1 AC3 5 GLU K  35  ASP K  40  0                                        
SHEET    2 AC3 5 ARG K   4  LEU K   9  1  N  ALA K   5   O  GLU K  35           
SHEET    3 AC3 5 LEU K  96  PRO K 102  1  O  ILE K  98   N  VAL K   8           
SHEET    4 AC3 5 LYS K 141  THR K 147  1  O  SER K 145   N  PHE K  99           
SHEET    5 AC3 5 GLN K 182  VAL K 183  1  O  GLN K 182   N  ALA K 142           
SHEET    1 AC4 5 GLU K  35  ASP K  40  0                                        
SHEET    2 AC4 5 ARG K   4  LEU K   9  1  N  ALA K   5   O  GLU K  35           
SHEET    3 AC4 5 LEU K  96  PRO K 102  1  O  ILE K  98   N  VAL K   8           
SHEET    4 AC4 5 LYS K 141  THR K 147  1  O  SER K 145   N  PHE K  99           
SHEET    5 AC4 5 GLN K 187  THR K 189  1  O  GLN K 187   N  LEU K 144           
SHEET    1 AC5 5 GLU L  35  ASP L  40  0                                        
SHEET    2 AC5 5 ARG L   4  LEU L   9  1  N  ALA L   5   O  GLU L  35           
SHEET    3 AC5 5 LEU L  96  PRO L 102  1  O  ILE L  98   N  VAL L   8           
SHEET    4 AC5 5 LYS L 141  THR L 147  1  O  SER L 145   N  PHE L  99           
SHEET    5 AC5 5 GLN L 182  VAL L 183  1  O  GLN L 182   N  ALA L 142           
SHEET    1 AC6 5 GLU L  35  ASP L  40  0                                        
SHEET    2 AC6 5 ARG L   4  LEU L   9  1  N  ALA L   5   O  GLU L  35           
SHEET    3 AC6 5 LEU L  96  PRO L 102  1  O  ILE L  98   N  VAL L   8           
SHEET    4 AC6 5 LYS L 141  THR L 147  1  O  SER L 145   N  PHE L  99           
SHEET    5 AC6 5 GLN L 187  THR L 189  1  O  GLN L 187   N  LEU L 144           
SHEET    1 AC7 5 GLU M  35  ASP M  40  0                                        
SHEET    2 AC7 5 ARG M   4  LEU M   9  1  N  ALA M   5   O  VAL M  37           
SHEET    3 AC7 5 LEU M  96  PRO M 102  1  O  ILE M  98   N  VAL M   8           
SHEET    4 AC7 5 LYS M 141  THR M 147  1  O  SER M 145   N  PHE M  99           
SHEET    5 AC7 5 GLN M 182  VAL M 183  1  O  GLN M 182   N  ALA M 142           
SHEET    1 AC8 5 GLU M  35  ASP M  40  0                                        
SHEET    2 AC8 5 ARG M   4  LEU M   9  1  N  ALA M   5   O  VAL M  37           
SHEET    3 AC8 5 LEU M  96  PRO M 102  1  O  ILE M  98   N  VAL M   8           
SHEET    4 AC8 5 LYS M 141  THR M 147  1  O  SER M 145   N  PHE M  99           
SHEET    5 AC8 5 GLN M 187  THR M 189  1  O  GLN M 187   N  LEU M 144           
SHEET    1 AC9 5 GLU N  35  ASP N  40  0                                        
SHEET    2 AC9 5 ARG N   4  LEU N   9  1  N  ALA N   5   O  GLU N  35           
SHEET    3 AC9 5 LEU N  96  PRO N 102  1  O  ILE N  98   N  VAL N   8           
SHEET    4 AC9 5 LYS N 141  THR N 147  1  O  SER N 145   N  PHE N  99           
SHEET    5 AC9 5 GLN N 182  VAL N 183  1  O  GLN N 182   N  ALA N 142           
SHEET    1 AD1 5 GLU N  35  ASP N  40  0                                        
SHEET    2 AD1 5 ARG N   4  LEU N   9  1  N  ALA N   5   O  GLU N  35           
SHEET    3 AD1 5 LEU N  96  PRO N 102  1  O  ILE N  98   N  VAL N   8           
SHEET    4 AD1 5 LYS N 141  THR N 147  1  O  SER N 145   N  PHE N  99           
SHEET    5 AD1 5 GLN N 187  THR N 189  1  O  GLN N 187   N  LEU N 144           
CISPEP   1 TYR G  128    ALA G  129          0        -0.39                     
CISPEP   2 ALA K  271    ARG K  272          0         6.05                     
CISPEP   3 ALA L  129    ALA L  130          0        10.38                     
SITE     1 AC1 22 HIS A  11  THR A  15  SER A  16  PHE A  17                    
SITE     2 AC1 22 ASN A  18  ALA A  20  PRO A 102  LEU A 103                    
SITE     3 AC1 22 GLN A 104  TRP A 105  PHE A 106  THR A 147                    
SITE     4 AC1 22 THR A 148  GLY A 149  GLY A 150  TYR A 155                    
SITE     5 AC1 22 ILE A 192  ARG A 200  ILE A 201  LEU A 204                    
SITE     6 AC1 22 GLN B  66  E6A B 302                                          
SITE     1 AC2 21 GLN A  66  PRO A  68  HIS B  11  THR B  15                    
SITE     2 AC2 21 SER B  16  PHE B  17  ASN B  18  ALA B  20                    
SITE     3 AC2 21 PRO B 102  LEU B 103  GLN B 104  TRP B 105                    
SITE     4 AC2 21 PHE B 106  THR B 147  THR B 148  GLY B 149                    
SITE     5 AC2 21 GLY B 150  TYR B 155  ILE B 192  ARG B 200                    
SITE     6 AC2 21 LEU B 204                                                     
SITE     1 AC3  9 TRP A 105  GLY A 149  GLY A 150  FAD A 601                    
SITE     2 AC3  9 PRO B  68  ALA B  69  TYR B 126  PHE B 178                    
SITE     3 AC3  9 GLN M 233                                                     
SITE     1 AC4 21 HIS C  11  THR C  15  SER C  16  PHE C  17                    
SITE     2 AC4 21 ASN C  18  ALA C  20  PRO C 102  LEU C 103                    
SITE     3 AC4 21 GLN C 104  TRP C 105  PHE C 106  THR C 147                    
SITE     4 AC4 21 THR C 148  GLY C 149  GLY C 150  TYR C 155                    
SITE     5 AC4 21 ILE C 192  ARG C 200  LEU C 204  GLN D  66                    
SITE     6 AC4 21 TYR D  67                                                     
SITE     1 AC5 20 GLN C  66  HIS D  11  THR D  15  SER D  16                    
SITE     2 AC5 20 PHE D  17  ASN D  18  ALA D  20  PRO D 102                    
SITE     3 AC5 20 LEU D 103  GLN D 104  TRP D 105  PHE D 106                    
SITE     4 AC5 20 THR D 147  THR D 148  GLY D 149  GLY D 150                    
SITE     5 AC5 20 TYR D 155  ILE D 192  ARG D 200  LEU D 204                    
SITE     1 AC6 21 HIS E  11  THR E  15  SER E  16  PHE E  17                    
SITE     2 AC6 21 ASN E  18  ALA E  20  PRO E 102  LEU E 103                    
SITE     3 AC6 21 GLN E 104  TRP E 105  PHE E 106  THR E 147                    
SITE     4 AC6 21 THR E 148  GLY E 149  GLY E 150  TYR E 155                    
SITE     5 AC6 21 ILE E 192  ARG E 200  LEU E 204  GLN F  66                    
SITE     6 AC6 21 PRO F  68                                                     
SITE     1 AC7 10 PRO E  68  ALA E  69  TYR E 126  TYR E 128                    
SITE     2 AC7 10 PHE E 178  TRP F 105  GLY F 149  GLY F 150                    
SITE     3 AC7 10 FAD F 301  GLN K 233                                          
SITE     1 AC8 23 GLN E  66  TYR E  67  PRO E  68  E6A E 602                    
SITE     2 AC8 23 HIS F  11  THR F  15  SER F  16  PHE F  17                    
SITE     3 AC8 23 ASN F  18  ALA F  20  PRO F 102  LEU F 103                    
SITE     4 AC8 23 GLN F 104  TRP F 105  PHE F 106  THR F 147                    
SITE     5 AC8 23 THR F 148  GLY F 149  GLY F 150  TYR F 155                    
SITE     6 AC8 23 ILE F 192  ARG F 200  LEU F 204                               
SITE     1 AC9 22 HIS G  11  THR G  15  SER G  16  PHE G  17                    
SITE     2 AC9 22 ASN G  18  ALA G  20  PRO G 102  LEU G 103                    
SITE     3 AC9 22 GLN G 104  TRP G 105  PHE G 106  THR G 147                    
SITE     4 AC9 22 THR G 148  GLY G 149  GLY G 150  TYR G 155                    
SITE     5 AC9 22 ILE G 192  ARG G 200  LEU G 204  GLN H  66                    
SITE     6 AC9 22 TYR H  67  E6A H 302                                          
SITE     1 AD1 20 GLN G  66  HIS H  11  THR H  15  SER H  16                    
SITE     2 AD1 20 PHE H  17  ASN H  18  ALA H  20  PRO H 102                    
SITE     3 AD1 20 LEU H 103  GLN H 104  TRP H 105  PHE H 106                    
SITE     4 AD1 20 THR H 147  THR H 148  GLY H 149  GLY H 150                    
SITE     5 AD1 20 TYR H 155  ILE H 192  ARG H 200  LEU H 204                    
SITE     1 AD2 10 TRP G 105  GLY G 149  FAD G 601  PRO H  68                    
SITE     2 AD2 10 ALA H  69  TYR H 126  TYR H 128  PHE H 178                    
SITE     3 AD2 10 GLN I 233  ALA I 234                                          
SITE     1 AD3 21 HIS I  11  THR I  15  SER I  16  PHE I  17                    
SITE     2 AD3 21 ASN I  18  ALA I  20  PRO I 102  LEU I 103                    
SITE     3 AD3 21 GLN I 104  TRP I 105  PHE I 106  THR I 147                    
SITE     4 AD3 21 THR I 148  GLY I 149  GLY I 150  TYR I 155                    
SITE     5 AD3 21 ILE I 192  ARG I 200  LEU I 204  HOH I 705                    
SITE     6 AD3 21 GLN J  66                                                     
SITE     1 AD4 21 GLN I  66  PRO I  68  HIS J  11  THR J  15                    
SITE     2 AD4 21 SER J  16  PHE J  17  ASN J  18  ALA J  20                    
SITE     3 AD4 21 PRO J 102  LEU J 103  GLN J 104  TRP J 105                    
SITE     4 AD4 21 PHE J 106  THR J 147  THR J 148  GLY J 149                    
SITE     5 AD4 21 GLY J 150  TYR J 155  ILE J 192  ARG J 200                    
SITE     6 AD4 21 LEU J 204                                                     
SITE     1 AD5 20 HIS K  11  THR K  15  SER K  16  PHE K  17                    
SITE     2 AD5 20 ASN K  18  ALA K  20  PRO K 102  LEU K 103                    
SITE     3 AD5 20 GLN K 104  TRP K 105  PHE K 106  THR K 147                    
SITE     4 AD5 20 THR K 148  GLY K 149  GLY K 150  TYR K 155                    
SITE     5 AD5 20 ILE K 192  ARG K 200  LEU K 204  GLN L  66                    
SITE     1 AD6 11 GLN E 233  ALA E 234  PRO K  68  ALA K  69                    
SITE     2 AD6 11 VAL K  72  TYR K 126  TYR K 128  PHE K 178                    
SITE     3 AD6 11 TRP L 105  GLY L 149  FAD L 301                               
SITE     1 AD7 21 GLN K  66  E6A K 602  HIS L  11  THR L  15                    
SITE     2 AD7 21 SER L  16  PHE L  17  ASN L  18  ALA L  20                    
SITE     3 AD7 21 PRO L 102  LEU L 103  GLN L 104  TRP L 105                    
SITE     4 AD7 21 PHE L 106  THR L 147  THR L 148  GLY L 149                    
SITE     5 AD7 21 GLY L 150  TYR L 155  ILE L 192  ARG L 200                    
SITE     6 AD7 21 LEU L 204                                                     
SITE     1 AD8 21 HIS M  11  THR M  15  SER M  16  PHE M  17                    
SITE     2 AD8 21 ASN M  18  ALA M  20  PRO M 102  LEU M 103                    
SITE     3 AD8 21 GLN M 104  TRP M 105  PHE M 106  THR M 147                    
SITE     4 AD8 21 THR M 148  GLY M 149  GLY M 150  TYR M 155                    
SITE     5 AD8 21 ILE M 192  ARG M 200  LEU M 204  GLN N  66                    
SITE     6 AD8 21 TYR N  67                                                     
SITE     1 AD9  7 GLN B 233  TYR M 126  PHE M 178  TRP N 105                    
SITE     2 AD9  7 GLY N 149  GLY N 150  FAD N 301                               
SITE     1 AE1 22 ASN M  64  GLN M  66  E6A M 602  HIS N  11                    
SITE     2 AE1 22 THR N  15  SER N  16  PHE N  17  ASN N  18                    
SITE     3 AE1 22 ALA N  20  PRO N 102  LEU N 103  GLN N 104                    
SITE     4 AE1 22 TRP N 105  PHE N 106  THR N 147  THR N 148                    
SITE     5 AE1 22 GLY N 149  GLY N 150  TYR N 155  ILE N 192                    
SITE     6 AE1 22 ARG N 200  LEU N 204                                          
CRYST1   95.600  210.770  228.080  90.00  90.00  90.00 P 21 21 21   56          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010460  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004745  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004384        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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